msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

233 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain (By similarity). Probably involved in protection against reactive chlorine species (RCS) generated by chlorite and hypochlorite (PubMed:25968643).

Belongs to the MsrQ family.

26.32 kDa

MTFQPTPRQLSAIKAALFLLTLLPALHYAHGLWSDSLGANPIEALTRGMGIWTLNFLFLTLCVSPLRKLSGWHWLLRLRRMLGLTAFAYGCLHLLTYLWLDQFWDVDAIARDIWKRPFITVGATAFLLMLPLALTSSHAAIRSLGGKRWQSLHRAVYAVAILGVVHYLWLVKRVALLDPIIYALVLAILLGWRVVERIRLNGPWPTRSTPPAVQPVVFMKRDAVAALGEPKKR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.815 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPMRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.815 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPMRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.797 kDa

MAAATGTRKKKTPRPGQWKLWLLYTAGFVPAVWTFYLGATGQLGADPVKTFEHLLGLWALRFLILTLLVTPIRDLTGITLLRYRRALGLLAFYYALMHFTTYMVLDQGLNLSAIITDIVRRPFITIGMISLALLVPLALTSNNWSIRKLGRRWSSLHKLVYIAIAGSAVHFLMSVKSWPAEPVIYAAIVAALLLWRLARPYLRTRKPALRPRGEAIALRK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

220 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.674 kDa

MAAAAQTGKKKTVRPGEWKIWLLYAVGFVPAVWTFYLGASGNLGADPVKTFEHTLGLWALRFLILTLMVTPIRDLTGMAFLRYRRALGLLAFYYALMHFATYMVLDQGLNISAIVTDIVRRPFITIGMISLVLLVPLALTSNNWSIRKLGRRWNSLHKLVYVAIAGGAIHFIMSVKSWPAEPVIYAGIVSALLLWRLVRPHARNRKPVSRPRGEAMAVKK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

219 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.855 kDa

MAAWMAGRQKWLLHPAAKPLIFMVCLLPFAWLFYAAWSDQLGANPAEALVRATGDWTLRFVCIVLAVTPLRVITRTPALARFRRMLGLFAYFYVVLHLLSYSWFDMGFDVADIARDIAKRPFILVGFSAFVLLTPLAATSFNAAIKAMGAKRWQLLHKLVYLIAGLGLLHFFWMRAGKNNFNEVFVYAAIVALLLGWRVWNHWAKARRRVSNNAAVGVH

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.768 kDa

MAKTSTSVIAAKTLVHAAALAPIALLGWQFWQVWQSGSDALGADPVAEIEHRTGLWALRLLLITLAITPLRQLTGQAVVIRFRRMLGLYAFFYATVHLAAYLTLDLRGFWTQIFEEILKRPYITVGFAAWLLLMPLAITSTQGWMRRLKRNWGRLHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILAVLLGWRVWKKLSARQTTARRSTPPPATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.755 kDa

MAKTSTSVIAAKTLVHAAALAPIALLGWQFWQVWQGGSDALGADPVAEIEHRTGLWALRFLLITLAITPLRQLTGQAVVIRFRRMLGLYAFFYASVHLAAYLTLDLRGFWTQIFEEILKRPYITVGFAAWLLLMPLAITSTQGWMRRLKRNWGRLHTLIYPIGLLAVLHFWWLVKSDIREPALYAGILAVLLGWRVWKKLSARRTTARRSTPPPATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.94 kDa

MAKKSVSVIAAKTAVHAAVLAPIALLGWQFWQVWQQGSDALGADPVAEIEHRTGLWALRLLLITLAITPLRQLTGQAVLIRFRRMLGLYAFFYASVHLTAYLWLDLRGFWTQIFEEIVKRPYITVGFTAWLLLVPLAITSTQGWMRRLKRNWGRLHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILALLLGWRVWKRLSARRTTARHSAPPPATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.97 kDa

MAKKSVSVIAAKTAVHAAVLAPIALLGWQFWQVWQQGSDALGADPVAEIEHRTGLWALRLLLITLAITPLRQLTGQAVLIRFRRMLGLYTFFYASVHLTAYLWLDLRGFWTQIFEEIVKRPYITVGFTAWLLLVPLAITSTQGWMRRLKRNWGRLHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILALLLGWRVWKRLSARRTTARHSAPPPATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.94 kDa

MAKKSVSVIAAKTAVHAAVLAPIALLGWQFWQVWQQGSDALGADPVAEIEHRTGLWALRLLLITLAITPLRQLTGQAVLIRFRRMLGLYAFFYASVHLTAYLWLDLRGFWTQIFEEIVKRPYITVGFTAWLLLVPLAITSTQGWMRRLKRNWGRLHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILALLLGWRVWKRLSARRTTARHSAPPPATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.858 kDa

MAKTSTSVIVAKTLVHAAALAPIALLGWQFWQVWQSGSDALGADPVAEIEHRTGLWALRFLLITLAITPLRQLTGQAVLIRFRRMLGLYAFFYATVHLAAYLTLDLRGFWTQIFEEILKRPYITVGFAAWLLLMPLAITSTQGWMRRLKRNWGRVHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILAVLLGWRAWKKLSARRTKARRSAPPQATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.858 kDa

MAKTSTSVIVAKTLVHAAALAPIALLGWQFWQVWQSGSDALGADPVAEIEHRTGLWALRFLLITLAITPLRQLTGQAVLIRFRRMLGLYAFFYATVHLAAYLTLDLRGFWTQIFEEILKRPYITVGFAAWLLLMPLAITSTQGWMRRLKRNWGRVHMLIYPIGLLAVLHFWWLVKSDIREPALYAGILAVLLGWRAWKKLSARRTKARRSAPPQATPR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

218 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

25.348 kDa

MMTFHPSPPQLTLIKSMLFIAALLPFGRLALFTLTDQLGANPIEFITRNTGDWTLYFLCMTLAITPLRRLSQWNWLIRLRRMLGLFAFFYACLHFTTFLWFDHFFDVNEMLKDVVKRPFITVGFSAFVLLIPLAITSTNGMVKRLGGKRWQWLHRLVYVIAALGILHYWWMKAGKHDFEQPIIFGTIVAVLLLVRVFWAWQKRSKNNALAGTSDCRTG

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

217 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.553 kDa

MLPSMLPPKSLRAVRIAVWLLALVPFLRLVVLGATDRYGANPLEFVTRSTGTWTLVLLCCTLAVTPLRRLTGMNWLIRIRRMLGLYTFFYGTLHFLIWLLVDRGLDPASMVKDIAKRPFITVGFAAFVLMIPLAATSTNAMVRRLGGRRWQWLHRLVYVTGVLGILHYWWHKAGKHDFAEVSIYAAVMAVLLGLRVWWVWRGARQGAIAGGAVPLRD

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

216 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.592 kDa

MRSLPALPKRLHGPSIWALYILGFLPAVWGFYLGATGRLPGNAVKEFEHLLGIWALRFLIATLAITPIRDLFGVNWLRYRRALGLLAFYYVMMHFLTYMVLDQTLLLPAIVADIARRPFITIGMAALVLLIPLAVTSNIWSIRRLGQRWNKLHRLVYVIAAAGALHFAMSVKVVGPEQMLYLFLVAVLVAWRAVRKRFLRWRRQGTAPMRSQARAG

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

215 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.422 kDa

MAFALSLPSLPKRYQPAAIWSLYVIGLCPGLWYFYLAATGGLGFNPVKDFEHLLGIWALRFLCLGLLVTPLRDLFNVNLIAYRRALGLIAFYYVLAHFTVYLVLDRGLILGSIAGDILKRPYIMLGMAGLIILIPLALTSNRWSIRRLGSRWNTLHKLVYLVLIVGVLHFVLARKSITLEPVFYISTMVVLLGYRLVRPSIMTMKRNKRARPVRT

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.954 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGLTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.983 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLAWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNQLRKQVHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.025 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.056 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWIILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKSRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.056 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWIILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKSRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.04 kDa

MRLTAKQVIWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQQLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.995 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.068 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.952 kDa

MRLTAKQVIWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFACATLHLTSYALLELGVNNLPLLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.995 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.068 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.952 kDa

MRLTAKQVIWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFACATLHLTSYALLELGVNNLPLLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.009 kDa

MRLTAKQVIWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.066 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFKRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.101 kDa

MRLTVKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSFFNRLRKQVHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.068 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.068 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.983 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLAWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNQLRKQVHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.027 kDa

MRLTAKQVIWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLMYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.997 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLAALLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQSMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQAHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.068 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.067 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVVILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNRLRKQVHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.052 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.08 kDa

MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYVKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFNRLRKQVHNKLSV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

211 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.983 kDa

MRLTAKQVTWLKVCLHLAGLLPFLWLAWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLLSLFNQLRKQVHNKLSL

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

210 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

24.051 kDa

MAEPRRKKRPSKLQDTLVYGLVWLACFAPLAWLAWRGYAGELGANPIDKLIRELGEWGLRLLLVGLAITPAARILKMPRLVRFRRTVGLFAFAYVALHLLAYVGIDLFFDWNQLWKDILKRPFITLGMLGFMLLIPLAVTSTNGWVIRMGRAAWSRLHRLVYLIVPLGVAHYYLLVKADHRPPIIYGAVFVALMLWRVWEGRRTASKSSP

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

210 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.769 kDa

MRYPFWRLAVFLAACVAPVWWLYQAWIFALGPDPGKVLVEDFGLATLVMLLITMSMTPLQRLTGWPGWIVVRRQLGLWCFAYVVLHMTMYALFILGLDLGQLGVELVKRPYIIVGALAFLGLLALAVTSNRYSQRRLGARWKKLHRLIYVILGLGLLHMFWIVRADLKEWALYAGIGAFLLLLRIPMITRRIPRLGGSAGTGSKKVQNNG

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

210 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.741 kDa

MRYPFWRLAVFLAACVAPVWWLYQAWIFALGPDPGKVLVENFGLATLVMLLITLAMTPLQRLTGWPGWIVVRRQLGLWCFAYVVLHMTMYALFILGLDWGQLGVELVKRPYIIVGALAFLGLLALAVTSNRYSQRRLGSRWKKLHRLVYVILGLGLLHMFWIVRADLKEWALYAGIGAILLLLRVPMIARRIPRLGGAAKAGSIKVQNNG

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

210 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.727 kDa

MRYPFLRLAVFLAACIAPVWWLYQAWIFALGPDPGKVLVENFGVATLVMLLITLSMTPLQRLTGWSGWIVVRRQLGLWCFAYALLHLSMYALFILGLDWGQLGVELVKRPYIIVGALALLGLLALAVTSNRYSQRRLGARWKKLHRIIYVILGLGLLHMFWIVRADLKEWALYAGIGAFLLLLRIPVFARRIPRLGGAAKARSVKVQNNG

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

208 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.164 kDa

MTGGSVLKDRDRLGRIAVFVACLLPLVWYGARFVGGDLGANPIEAFTRKLGEWGLIFLLASLAATPARLLWGWTFPLRRRRMVGLFAFFYVCLHLLSYIGLDQFFDWGAIWADIVKRTYITVGMAALLLLVPLAVTSTRGMVRRLGGKRWIALHRLVYPAAVLGVLHYMLMVKADLSEPLIFAGILGLLLAVRLVPAVRRRRSGRAPS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.798 kDa

MRLTQKQIVWLKVLLHLAGLLPFLWLVWAVNQGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGINNLALLGQELITRPYLTLGIISWFILFALTLTSTQAAQRKLGKRWQRLHNFVYLVAILAPIHYLWSVKILSPQPVIYALLALVLLAWRYKTFRQWWRSFAGKML

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.238 kDa

MPAAPLTARAIGRIKPLLFVAGLLPFARWFWLGANDGLSANPVEFLTRSSGTWTLVCLLVTLAITPLRRLTGQPALVRLRRMCGLFAFFYGSLHFLAWVWWDRGLDPVSMLQDVGERPFITVGFAAFVLMAALAATSTQWAMRKLGKRWQVLHRAVYAIGLLAILHFWWHKAGKNDLQQPLLYGSVLALLLGWRVAAWWRRRGAAR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.238 kDa

MPAAPLTARAIGRIKPLLFVAGLLPFARWFWLGANDGLSANPVEFLTRSSGTWTLVCLLVTLAITPLRRLTGQPALVRLRRMCGLFAFFYGSLHFLAWVWWDRGLDPVSMLQDVGERPFITVGFAAFVLMAALAATSTQWAMRKLGKRWQVLHRAVYAIGLLAILHFWWHKAGKNDLQQPLLYGSVLALLLGWRVAAWWRRRGAAR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.24 kDa

MPAAPLTARAIGRIKPLLFVAGLLPFARWFWLGANDGLSANPVEFLTRSSGTWTLVCLLVTLAITPLRRLTGQPALVRLRRMCGLFAFFYGSLHFLAWVWWDRGLDPVSMLQDVGERPFITVGFAAFVLMAALAATSTQWAMRKLGKRWQTLHRAVYAIGLLAILHFWWHKAGKNDLQQPLLYGSVLALLLGWRVAAWWRRRGAAR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.851 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQWFR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.653 kDa

MLSLFRIIIHVCCLGPVAWLAWVLLSGDESQLGADPIKEIQHFLGFSALTILLIMFILGKVFYLLKQPQLQVLRRALGLWAWFYVVLHVYAYLALELGYDFSLFVQELVNRGYLIIGAIAFLILTLMALSSWSYLKLKMGKWWFYLHQLGYYALLLGAIHYVWSVKNVTFSSMLYLILSIMILCDALYGLFIKRKGRSTSAHTGKD

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

206 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.346 kDa

MRYPIWRVGVFIAAAVWPLFWLYEAWSAVLGPDPGKVLVDRLGLGTLILLLITLAMTPLQKLSGWAGWIAVRRQLGLWCFAYVVLHLAAYCVFVLGLDWSQLGVELRKRPYIIVGALGFLLLLVLAVTSNRYSQRRLGSRWKKLHRLVYVVLGLGLLHMLWIVRADLKEWAIYASIGALLLVLRIPPVMRRIPRLIAKKPLSATKA

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

204 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.467 kDa

MRYPWLRLAIFIVGCLFPLWWLYEAAMNLLGPDPGKILMDRLGLGALIFLLITLSMTPLQKLTGWSGWIVVRRQLGLWCFAYIVLHLLCYLFFILGLDWGQFAVELRKRPYIIVGALGFIGLLALAVTSNRYSQRRLGGRWKKLHKLVYVILGLGLLHFLWIVRSDLREWAIYAVIGGFLMVLRVPAVARRVPRIMGRRGRVAS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

203 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.361 kDa

MRLSLRHITWLKIAIWLAATLPLLWLVLSINLGGLSADPAKDIQHFTGRMALKLLLATLLVSPLARYSKQPLLLRCRRLLGLWCFAWGTLHLLSYSILELGLSNIGLLGHELINRPYLTLGIISWLVLLALALTSTRWAQRKMGARWQKLHNWVYVVAILAPIHYLWSVKTLSPWPIIYAVMAALLLLLRYKLLLPRYKKFRQ

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

203 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.282 kDa

MRYPWFRLAIFVLGCLFPLWWFYEAAMGLLGPDPGKIMMDRLGLGALVFLLITLSMTPLQRLTGWSGWIVVRRQLGLWCFAYIVLHLVSYLVFILGLDWGQFGVELRKRPYIIVGALGFLGLLALAVTSNRYSQRRLGARWKKLHRLVYVILGLGLLHFLWIVRSDLKEWAIYAGIGGVLLVMRIPPVWRRVPRLMGGRGRAA

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

203 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.261 kDa

MRYPWFRLAIFVVGCLFPVWWLYEAAMNLLGPDPGKIMMDRLGLGALTFLLVTLSMTPLQKLTGWSGWIVVRRQLGLWVFAYIVLHILAYLFFILGLDWGQLAVELRKRPYIIVGALGFLGLLALAVTSNRYSQRRLGARWRKLHRLVYAVLGLGLLHFLWIVRSDLREWAIYAFIGAVLMVLRIPAVARALPRVARKQGRAV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

203 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.175 kDa

MRYPWFRLAIFVVGCLFPAWWLYEAAMSLLGPDPGKIMMDRLGLGALTFLLVTLCMTPLQKLTGWSGWIVVRRQLGLWVFAYIVLHILAYLFFILGLDWGQLAVELRKRPYIIVGALGFLGLLVLAITSNRYSQRRLGARWKKLHRLVYAVLGLGLLHFLWIVRSDLREWSIYALIGAVLMVLRIPAVARGLPRVARARGRAV

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.026 kDa

MARRPPPYAWLGPGVVLGGLLPTVFLLWDALSGGLGANPVKQATHQTGQLALIVLTLSLACTPARVWLGWTWAARIRKALGLLAAFYAVLHFGIYLRGQDFSLGRIWEDVTERPFITSGFAALLLLLPLVLTSGKGSVRRLGFARWTLLHRLVYLAAALGALHYWWGVKKDHSGPLLAVLVLAALGLARLKTPARLNRPARQ

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.406 kDa

MRFTVKQIVWLKVLLHLAGFLPLVWLFWAGHQGYFSADPAKDIQHFTGRMALKFLLATLLVSPLARYAKQPLLIRVRRLLGLWCFAWATLHLTSYTLLELGINNLALLGSEIITRPYLTLGMISWAILLALAVTSTQAMQRKLGRRWQLLHNFVYLVAILAPIHYLWSVKIVSPQPVVYALLAAGLLTWRYKKFRQWWRAIR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.049 kDa

MRYWYLRLAVFLGALAMPAWWLYQAWIFALGPDPGKTLVDRLGLGALVLLLLTLAMTPLQKLSGWPGWIAVRRQLGLWCFTYALLHLSAYCVFILGLDWGQLGIELSKRPYIIVGMLGFICLFLLAITSNRFAMRKLGSRWKKLHRLVYLILGLGLLHMLWVVRADLEEWTLYAVVGASLMLLRLPSIARRLPRLRGRPGVS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.089 kDa

MRYWYLRLAVFLGALAVPAWWLYQAWIFALGPDPGKTLVDRLGLGALVLLLLTLAMTPLQKLSGWPGWIAVRRQLGLWCFTYVLLHLSAYCVFILGLDWGQLGIELSKRPYIIVGMLGFICLFLLAITSNRFAMRKLGSRWKKLHRLVYLILGLGLLHMLWVVRADLEEWTLYAVVGASLMLLRLPSIARRLPRLRTRPGVS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.075 kDa

MRYWYLRLAVFLGALAVPAWWLYQAWIFALGPDPGKTLVDRLGLGALVLLLLTLAMTPLQKLSGWPGWIAVRRQLGLWCFTYVLLHLSAYCVFILGLDWGQLGIELSKRPYIIVGMLGFVCLFLLAITSNRFAMRKLGSRWKKLHRLVYLILGLGLLHMLWVVRADLEEWTLYAVVGASLMLLRLPSIARRLPRLRTRPGVS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

202 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.175 kDa

MRYWYLRLAVFLGALAVPAWWLYQAWIFALGPDPGKTLVDRLGLGALVLLLLTLAMTPLQKLSGWPGWIAVRRQLGLWCFTYVLLHLSAYYVFILGLDWGQLGIELSKRPYIIVGMLGFVCLFLLAITSNRFAMRKLGSRWKKLHRLVYLILGLGLLHMLWVVRADLEEWTLYAVVGASLMLLRLPSIARRLPRLRTRHGVS

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

200 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.992 kDa

MRLTAKQITWLKVALHLAAFLPLVWLFYAASQGLFRADPAKDIQHFTGRMALKLLLATLLVTPLTRLLKQPLLIRTRRLLGLWCFAWATLHLVSYSLLELGLSNLSLLGSELVSRPYLTLGIVSWLILLALALTSFQAAQRKLGRRWQTLHNFIYLVAILAPIHYLWSVKILSPQPVLYALGAIVLLAWRYKKLRQWWRT

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.855 kDa

MRLTAKQIIWLKVCLHLVGFLPLLWLFWAINQGGLSADPVKDIQHFTGRTALKFLLATLLISPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLALLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPVHYLWSVKVLSPQPVIYAALALVLLALRYRKFRQWRR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.898 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYATLALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRRFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.873 kDa

MRLTPTHIKGIKVAIYLAAFLPFLWLVLSVDQGWFSADPAKDIQHFTGRMTLKLLLATLMIAPLARYTRQPLLIRCRRLVGLWCFAWGTLHLISYSTLELGLSNIGLLGRELVTRPYLTLGIISWLILLALAATSTLWAMRKLGAKWQTLHNLVYLVAILAPIHYLWSVKTFSPQPFIYALLAVVLLALRYKKFRNWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.855 kDa

MRLTAKQIIWLKVCLHLVGFLPLLWLFWAINQGGLSADPVKDIQHFTGRTALKFLLATLLISPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLALLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPVHYLWSVKVLSPQPVIYAALALVLLALRYRKFRQWRR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.898 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYATLALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRRFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.896 kDa

MRLTVKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.868 kDa

MRLTAKQITWLKVCLHLAGFLPLLWLFWAINHGGLSADPVKDIQHFTGRTALKFLLATLLVSPLARYAKQPLLIRTRRLLGLWCFVWATLHLTSYALLELGIHNLALLGSELISRPYLTLGIISWLVLLALTLTSTQFAQRKLGKRWQTLHNVVYLVAILAPIHYLWSVKILSPQPVIYAALALALLALRYRKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.873 kDa

MRLTPTHIKGIKVAIYLAAFLPFLWLVLSVDQGWFSADPAKDIQHFTGRMTLKLLLATLMIAPLARYTRQPLLIRCRRLVGLWCFAWGTLHLISYSTLELGLSNIGLLGRELVTRPYLTLGIISWLILLALAATSTLWAMRKLGAKWQTLHNLVYLVAILAPIHYLWSVKTFSPQPFIYALLAVVLLALRYKKFRNWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.815 kDa

MRLTLRQIKWLKVAIWLAAALPFLWLILSVDQGWFSADPAKDIQHFTGRMTLKLLLATLLVTPLARYGKQPLLIRCRRLLGLWCFAWGTLHLVSYSVLELGLSNIGLLGRELVTRPYLTLGIISWLLLLSLAVTSTLWAQRKMGANWQKLHNLVYVVAILAPIHYLWSVKTLSPLPIIYAVTAAILLALRYKKFRQWCR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.152 kDa

MRLTAKQITWLKVILHLAGLLPFIWLFWAASQGYFSADPAKDIQHFTGRMALKFLLASLLISPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGINNLALLGSELISRPYLTLGIVSWVILFALTLTSTQYAQRKLGRRWQFLHNFVYLVAILTPIHYLWSVKILSPQPVIYALLALGLLAWRYKKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.778 kDa

MRLTAKQVIWLKVCLHLAGFLPFVWLAWAINHGGLSADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALFGQELITRPYLTLGIVSWLILLALAFTSTQAMQRNLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPILYAGLALLLLALRYKKFRTWLK

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.084 kDa

MRFTVKQIAWLKVFLHLAGFLPLVWLFWAGHQGYFSADPAKDIQHFTGRMALKFLLATLLVAPLARYAKQPLLIRIRRLLGLWCFAWATLHLTSYTLLELGINNLALLGSEIINRPYLTLGMICWVILLALAATSTQAMQRKLGRRWQLLHNFVYLVAILAPIHYLWSVKIVSPQPIIYALLAVVLLACRYKKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.109 kDa

MRLTLQHINRLKVLLHLAGFLPLLWLILSVDQGWFSADPAKDIQHFTGRMALKLLLATLLVTPLARYGKQPLLIRCRRLLGLWCFFWATLHLVSYALLELGLDHLALLGKELISRPYLTLGIISWLILLALAVTSPQIMMRKLGSQWQKLHNFVYLVAILTPIHYLWSVKTLSPQPILYALAALILLLLRYKKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

199 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

23.086 kDa

MRLTLQHITRLKVLLHLAGFLPLLWLILSVDQGWFSADPAKDIQHFTGRMALKLLLATLLVTPLARYGKQPLLIRCRRLLGLWCFFWATLHLVSYALLELGLDHLALLGKELISRPYLTLGVISWLILLALAVTSPQIMMRKLGSQWQKLHNFVYLVAILAPIHYLWSVKTLSPQPILYALAALILLLFRYKKFRQWWR

msrQ

Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ

197 amino acids

Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.

Belongs to the MsrQ family.

22.64 kDa

MRYPWFRLAIFIVGCLFPVWWLYEAAMNLLGPDPGKIMMDRLGLGALTFLLVTLSMTPLQKLTGWSGWIVVRRQLGLWVFAYIVLHILCYLFFILGLDWGQLAVELRKRPYIIVGALGFLGLLVLAVTSNRYSQRRLGARWKKLHRLVYAVLGLGLLHFLWIVRSDLREWAIYAFIGAVLMVLRIPAVARALPKVAR