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msrP

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Yersinia pestis
Length
366 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
40.979 kDa
Sequence
MHNTFTHTKNNTHTKNNTQAKNSGSQTKSNAVSLNKPRKLTEADVTPESIFYQRRKVLQALGITAATLALPASAQADLLAWFKGNEPPKAPSGKPLTFTPSAAYHPDLALTPEDKVTGYNNFYEFGLDKADPAANAGTLKTEDWQIKIDGDVVKPMTLDMDYLMKCFPLEERIYRLRCVEAWSMVVPWIGFELGKLLKLAEPTSNARYVAFQTLYAPDQMPGQKNRFIGGGLDYPYVEGLRLDEAMHPLAFMVVGVYGKTLPPQNGAPLRLMTPWKYGFKSIKSIVHIRLTRDQPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERVIGSGGILDVKRQPTLLFNGYAEQVASLYRGLDLRKNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
366 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
40.965 kDa
Sequence
MHNTFTHTKNNTHTKNNTQAKNSGSQTKSNAVSLNKPRKLTEADVTPESIFYQRRKVLQALGITAATLALPASAQADLLAWFKGNEPPKAPSGKPLTFTPSAAYHPDLALTPEDKVTGYNNFYEFGLDKADPAANAGTLKTEDWQIKIDGDVVKPMTLDMDYLMKCFPLEERIYRLRCVEAWSMVVPWIGFELGKLLKLAEPTSNARYVAFQTLYAPDQMPGQKNRFIGGGLDYPYVEGLRLDEAMHPLAFMVVGVYGKTLPPQNGAPLRLMTPWKYGFKSIKSIVHIRLTRDQPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERVIGSGGILDVKRQPTLLFNGYADQVASLYRGLDLRKNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
361 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
39.622 kDa
Sequence
MTDPDSTSPAPDPQQPADPQPTDPGRREVLRQGALLTATALGLGGGLTLLTRRPAPAEPAPDPQTAAGRVIRPTGPYDTQEAMTGYRDMTTYNNFYELGLGKDDPARHAGALPTRPWTVVVDGEVKKPVTLDIDTLQSWFPLEDRIYRMRCVEGWSMVMPWFGFPLAALLRRLEPTGAARYVQFTAINAPDKLPGQRPWVLEWPYTEGLRLDEALHPLTLLAVGLEGRSLPAQNGAPLRLVVPWKYGFKGIKAIVRMTLTRTQPQTTWALAAPDEYGFYANVNPAVPHPRWSQATEQRIGESGRRPTLPFNGYGEQVAGLYSGLDCGGTSKWRAARPPMRGSVQASCWAGYSPPFSCCGTR

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
337 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
38.144 kDa
Sequence
MLIKIPSRSDCSESEVTSETLYLSRRRLLGASFAGLALASGLPRLGFADEQRYAGVESVPAPGWFAEKLPQTRWQAVNVQGEAITPFKDATHYNNFYEFGPNKGDPAENASALKAEPWSVVIDGEVGKPGTYALEDFVKPYQLEERIYRLRCVEAWSMVIPWLGFPLADLLKRVEPNGQAKFVRFETLQRPEQMVGQRSGFSVIDWPYMEGLRMDEAMHPLAILAVGMYGRLLPNQNGAPLRLVVPWKYGFKSIKSIVRISLVREQPKTTWESIAANEYGFYANVNPQVDHPRWSQARERRLPSGLFSPNVRDTQMFNGYGSEVASLYSGMDLRKYY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Length
337 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.688 kDa
Sequence
MLIKLPRSSECKASEITPEGIYLSRRTLLGGSLAGLALGALPGGVGAAQMSRYADVQAGAAPAWFTDKLAATRWQAVTVKDEAITPFKDATHYNNFYEFGPDKGDPAANGDSLKTEPWSIVVDGEVRKPGRYALEDFVKPYQLEERIYRLRCVEAWSMVIPWLGFPLAQVLKQVEPTSSARYVRFETLKDPQHMPGQRSGFALIDWPYREGLRLDEAMHPLAILAVGMYGRELPNQNGAPLRLVVPWKYGFKSIKSIVRISLVAEQPGTTWEGLAPDEYGFYANVNPTVDHPRWSQARERRLPSGLFSPNVRETQMFNGYADEVASLYTGLDLRKNY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Length
337 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.88 kDa
Sequence
MLIKLPSASGSKESDVTPESIYLSRRTLLASSLAGLAVTALPRWASAADASRYADVEAGKAPGWFADKLPSTQWQAVTVKDEAITPFKDATHYNNFYEFGTDKGDPAKNAGSLKTEPWTVVIDGEVGKPGRYALEDFMKPYQLEERIYRLRCVEAWSMVIPWIGFPISALLKQVEPTSKAKYIRFETLEDAKSMPGQRSDFALIDWPYVEGLRLDEAMNPLAILAVGMYGRELPNQNGAPLRLVVPWKYGFKSVKSIVRISLVSEQPKTTWQSIAANEYGFYANVNPMVDHPRWTQARERRLPSGLFSPNLRETKMFNGYEEEVGSLYAGMNLRKDY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.478 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSVVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella typhi
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.411 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.367 kDa
Sequence
MKKNQFLKESDITAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDTWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGLQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTREHPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Shigella sonnei (strain Ss046)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.441 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPTAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.16 kDa
Sequence
MKKVSRLTEADVTAESAFFMQRRQVLKALGITTAALSLPTAAHADVLSWFKGNDRPKAPAGAPLDFTRPAQYQAKLDLTPEDKVTGYNNFYEFGLDKADPAANAGSLKTNPWTLKIGGEVAKPLTLDHDDLTKKFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALVEPTSNAKYVAFKTLYAPDIMPGQKDRFIGGGLEYPYVEALRLDEAMHPLTMLTTGVYGKALPPQNGAPVRLTVPWKYGFKGIKSIVSITLTRERPPTTWNMAAPDEYGFYANVNPHVDHPRWSQASERVIGSGGVLDVKRQPTLLFNGYADEVASLYKGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.425 kDa
Sequence
MKKKQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.314 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTSERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.37 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILNVQRQPTLLFNGYAEQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain 55989 / EAEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.371 kDa
Sequence
MKKNQFLKESDVTAESVFFMTRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNDLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYAEQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O157:H7
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.357 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.357 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.417 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAAFSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella agona (strain SL483)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.478 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSVVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.491 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLLSWFKGNDRPKAPVGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPYTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLTQAQPTSHAKYVAFETLYAPDDMPGQKDRFVGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYASEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella choleraesuis (strain SC-B67)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.478 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSVVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella dublin (strain CT_02021853)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.508 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPLTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.508 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPLTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.508 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPLTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella heidelberg (strain SL476)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella newport (strain SL254)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.492 kDa
Sequence
MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQADLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O81 (strain ED1a)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.383 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O8 (strain IAI1)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.425 kDa
Sequence
MKKKQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.413 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISATALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPYVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O9:H4 (strain HS)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.427 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPLAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O1:K1 / APEC
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.37 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILNVQRQPTLLFNGYAEQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.445 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAAFSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLVAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.383 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain K12)
Length
334 amino acids
Function
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons (PubMed:26641313). Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine (PubMed:26641313). 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 (PubMed:26641313). The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (PubMed:26641313). Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides (PubMed:15355966). Shows no activity as sulfite oxidase (PubMed:15355966).
Similarity
Belongs to the MsrP family.
Mass
37.369 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISATALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPYVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYAAQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.331 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNDLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRECPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain SE11)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.425 kDa
Sequence
MKKKQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.411 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.37 kDa
Sequence
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILNVQRQPTLLFNGYAEQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.222 kDa
Sequence
MKAVNPLTENDVTPESLFNARRRTVLKMLGMSAAALSLPGAARADLLSWFKGGDRPRAASGRPLDFSQPQQFQANLPLTPEDKVTGYNNFYEFGLDKADPAAHAGTLKTADWKIEIDGEVAKPLTLSMDDIFKRFAQEQRIYRMRCVEGWSMVVPWVGFELGKLLQAAEPTSNARFVAFHTLYAPDQMPGQQDRFIGGGLDYPYVEGLRLDEAMHPLTLLTTGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVKISLVKAMPPTTWNQLAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
334 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.284 kDa
Sequence
MKKIRKLTEADVTAESAFFMQRRQVLKALGISAAALSLPNAAHADLLSWFKGNDRPPAPAGKPLEFSKPTAWQNNLPLTPEDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDALTRRFPLEERIYRMRCVEAWSMVVPWIGFPLNKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGAGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Serratia proteamaculans (strain 568)
Length
333 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.551 kDa
Sequence
MSKQRKLTEADVTPESVFYQRRKVLQALGITAASLALPHNAQADLLSWFKGNDRPKAPPGKPLEFSKPAAWQAQLDLTPEDKVTGYNNFYEFGLDKADPAANAGGLKTEGWQVRIDGEVAKPITLDIDDLIKRFPLEQRIYRMRCVEAWSMVVPWIGFELGKLIKFAEPNSNARYVAFQTLYDPEQMPGQKDRFIGGGLKYPYVEGLRLDEAMNPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIKSIVHIRLVRDQPPTTWNQSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVKRQPTLLFNGYAEQVASLYRGLDLRENF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
333 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.469 kDa
Sequence
MHKHRKPTEADVTPESLFYQRRRVLKALGISAAALSLPLSAQADLLAWFKGSDKPKAPPGKPLTFSQPTDWKLDLPLTPEDKVTGYNNFYEFGLDKADPAANAGGLKTDGWTIKIDGDVAKPLTLDIDDLLKRFPLEERIYRFRCVEAWSMVIPWVGFELAKLIKFAEPTSNARYVAFQTLHDPEQMPGQKDRFMGGGLDYPYVEGLRMDEAMNPLALLAVGVYGKTLPPQNGAPIRLVTPWKYGFKNIKSIVHIRLTRERPPCTWNLAAPDEYGFYANVNPHVDHPRWSQATERVIGSGGLLNVERQPTLLFNGYAEQVASLYRGLNLRDNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
333 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.547 kDa
Sequence
MHKHRKPTEADVTPESLFYQRRRILKALGISAAALSLPFSAQADLLAWFKGTDKPKAPPGKPLTFSQPADWKLDLPLTPEDKVTGYNNFYEFGLDKADPAANAGGLKTEGWTIKIDGDVAKPLTLDIDDLLKRFPLEERIYRFRCVEAWSMVIPWVGFELAKLIKFAEPTSNARYVAFQTLYDPEQMPGQKDRFMGGGLDYPYVEGLRMDEAMNPLALLAVGVYGKTLPPQNGAPIRLVTPWKYGFKNIKSIVHIRFTREKPPCTWNLAAPDEYGFYANVNPHVDHPRWSQATERVIGSGGLLNVERQPTLLFNGYAEQVASLYRGLNLRDNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Burkholderia mallei (strain ATCC 23344)
Length
331 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.121 kDa
Sequence
MLIKKTLRAALAGDDIPRSEITPRAVFEHRRRILQAAGAAAAGGLVGAHGLALAAYASPDATARKLAAPANPKFVVPEKVTSFKDITTYNNFYEFGTDKSDPARRAGTLRPHPWRVSVEGEVRNPKVYDIDALLKLAPLEERVYRLRCVEGWSMVIPWIGFPLAELIKRVEPTANAKYVQFVTLADPSQMPGLSAPILDWPYSEGLRMDEAMNPLTLLTIGVYGQVLPNQNGAPVRVIVPWKYGFKSAKSIVKIRFVDRQPPTSWNTYAPNEYGFYSNVNPNVDHPRWSQATERRIGEDGFFTPKRKTLMFNGYGDWVASMYRGMDLKKYF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Burkholderia pseudomallei (strain K96243)
Length
331 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.091 kDa
Sequence
MLIKKTLRAALAGDDIPRSEITPRAVFEHRRRILQAAGAAAAGGLVGAHGLALAAYASPDAAARKLAAPANPKFVVPEKVTSFKDITTYNNFYEFGTDKSDPARRAGTLRPHPWRVSVEGEVRNPKVYDIDALLKLAPLEERVYRLRCVEGWSMVIPWIGFPLAELIKRVEPTANAKYVQFVTLADPSQMPGLSAPILDWPYSEGLRMDEAMNPLTLLTIGVYGQVLPNQNGAPVRVIVPWKYGFKSAKSIVKIRFVDRQPPTSWNTYAPNEYGFYSNVNPNVDHPRWSQATERRIGEDGFFTPKRKTLMFNGYGDWVASMYRGMDLKKYF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Ralstonia solanacearum (strain GMI1000)
Length
331 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
37.302 kDa
Sequence
MLIKTDRWLRGDDIPASEITPQHLFDQRRRLLAAAALGAAGAALSPWAARRAFAASPAPAWLAAKPNPAYATVEKPTPFDEVTTYNNFYEFGTDKSDPARYAGTLRPHPWQVSVEGLVKAPKTYDLDDLMKMAPMEERIYRLRCVEGWSMVIPWVGFPLAELIRRVEPQGSARYIQFISLADKRQMPGVSSPVLDWPYSEGLRMDEAMHPLVLLTFGLYGQVLPNQNGAPVRVIVPWKYGFKSAKSIVRIRFVDKQPPTSWNIAAPNEYGFYSNVNPSVDHPRWSQATERRIGEDKGGFGGLFAPKRKTLMFNGYDQVASLYTGMDLRKFF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
322 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.143 kDa
Sequence
MSFRDALNLPSSEITDESVYRDRRRLLQLLALTPALGVAGCAEADPPPPPKTVVTPAQARSGFRTAEELTRLEDVTSYNNFYEFGTDKTDPSKAAKTLKLSPWTVKVGGECEKPGSLSLDELLKGIASEERIYRLRCVEGWSMVIPWTGVPLGEVLKRFAPTSKAKYVAFTTLADPQQMPGVRYRSINWPYREGLRIDEAMHPLTLLATGLYGKPLPQQNGAPLRLVVPWKYGFKSIKSIVEIRFVEKMPETAWHDLQPSEYGFFSNVNPAVDHPRWSQKTERRIAGTASKLFAERIATKPFNGYADQVASLYAGMDLKKWF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
322 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.204 kDa
Sequence
MSLRDALKTPSSEITDEAVYRDRRRLLQLFALTPALSVAGCAEADPPPPPKTVVTPAQARSGFRTAEELTRLEDVTSYNNFYEFGTDKTDPSKAAKTLKLSPWSVKVSGECEKPGSLSLDELLKGISAEERIYRLRCVEGWSMVIPWTGVPLGEVLKRFAPTSRAKYVAFTTLADPQQMPGVRYRSINWPYREGLRIDEAMHPLTLLATGLYGKPLPQQNGAPLRLVVPWKYGFKSIKSIVEIRFVEKMPETAWHDLQPSEYGFFSNVNPAVDHPRWSQKTERRIAGTASKLFAERIATKPFNGYADQVASLYAGMDLKKWF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
319 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.416 kDa
Sequence
MSSFKPSRFSTARLTGDAVTPKSIYLRRREFMIGLGAIAATGAASSAFADPLEAKTTAYKVDEKLTPQNAVTTYNNFYEFGTDKSDPSANSGSFKPLPWKLTVDGLVKQPKEFDVEELIAKMPLEERIYRMRCVEAWSMVIPWIGFPLSSLLSQVEPLGSAKYIAFTGVVRPDEMPGQTGLFQALNWPYVEGLRLDEAMHPLTILSVGLYGETLPNANGAPIRLVVPWKYGFKGIKAITRISFVEKQPPTSWNRQAANEYGFYANVNPAVDHPRWSQATERRIGEGGFFGSDRRPTLPFNGYGEEVASLYAGMDLKANY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Brucella suis biovar 1 (strain 1330)
Length
319 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.416 kDa
Sequence
MSSFKPSRFSTARLTGDAVTPKSIYLRRREFMIGLGAIAATGAASSAFADPLEAKTTAYKVDEKLTPQNAVTTYNNFYEFGTDKSDPSANSGSFKPLPWKLTVDGLVKQPKEFDVEELIAKMPLEERIYRMRCVEAWSMVIPWIGFPLSSLLSQVEPLGSAKYIAFTGVVRPDEMPGQTGLFQALNWPYVEGLRLDEAMHPLTILSVGLYGETLPNANGAPIRLVVPWKYGFKGIKAITRISFVEKQPPTSWNRQAANEYGFYANVNPAVDHPRWSQATERRIGEGGFFGSDRRPTLPFNGYGEEVASLYAGMDLKANY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Pasteurella multocida (strain Pm70)
Length
319 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.497 kDa
Sequence
MHKLNENDVTPEHIFFERRKIIQSMGLMGAASLLPRFSLAAEKQDSRQALHFAKDHNPQNLLLTPENKVIGYNNFYEFGVDKASPAKYASALKTEPWTLRIEGEVEKPMTFDVHQLMQQLPLEERIYRFRCVEAWSMVIPWIGFELNKLLALVQPTSQAKYVEFETLYEPDSMPGQKNHFFGGGLIYPYVEGLTMAEAMHPLTLLSVGLYGKTLAPQNGAPIRLVVPWKYGFKNIKSIVKITLKSEQPMTTWHHAAPHEYGFYANVNPEVDHPRWSQASERVIGSGGLLSVKRQPTLLFNGYAEQVAHLYQDLDLRTYF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
318 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.11 kDa
Sequence
MNRFTRYDVTPEAIFNQRRQIIKAMGLGAAALSLPNIGFAAEKSDQLKALNFKDAPKGDFLLTPENKVTGYNNFYEFGVDKASPAKFAKDFKTDPWSLEIAGEVENPFVLNHAQLFNTFPLEERIYRFRCVEAWSMVIPWVGFELARLVEMAKPTSKAKFVIFHTLHDPEQMPGQKNKFFGGGIDYPYVEALTIEEAMNPLTLLSVGLYGKMLPPQNGAPIRLVVPWKYGFKSIKSIVKITFSETRPRTTWEKLAPHEYGFYANVNPNVDHPRWSQASERVIGSGGLLAVKRQDTLMFNGYEKEVAHLYKGLDLKVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
318 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.11 kDa
Sequence
MNRFTRYDVTPEAIFNQRRQIIKAMGLGAAALSLPNIGFAAEKSDQLKALNFKDAPKGDFLLTPENKVTGYNNFYEFGVDKASPAKFAKDFKTDPWSLEIAGEVENPFVLNHAQLFNTFPLEERIYRFRCVEAWSMVIPWVGFELARLVEMAKPTSKAKFVIFHTLHDPEQMPGQKNKFFGGGIDYPYVEALTIEEAMNPLTLLSVGLYGKMLPPQNGAPIRLVVPWKYGFKSIKSIVKITFSETRPRTTWEKLAPHEYGFYANVNPNVDHPRWSQASERVIGSGGLLAVKRQDTLMFNGYEKEVAHLYKGLDLKVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
318 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.138 kDa
Sequence
MNRFTRYDVTPEVIFNQRRQIIKAMGLGAAALSLPNIGFAAEKSDQLKALNFKDAPKGDFLLTPENKVTGYNNFYEFGVDKASPAKFAKDFKTDPWSLEIAGEVENPFVLNHAQLFNTFPLEERIYRFRCVEAWSMVIPWVGFELARLVEMAKPTSKAKFVIFHTLHDPEQMPGQKNKFFGGGIDYPYVEALTIEEAMNPLTLLSVGLYGKMLPPQNGAPIRLVVPWKYGFKSIKSIVKITFSETRPRTTWEKLAPHEYGFYANVNPNVDHPRWSQASERVIGSGGLLAVKRQDTLMFNGYEKEVAHLYKGLDLKVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
318 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.057 kDa
Sequence
MKQLMMSDVTPEEIFNQRRQIIKSMGLGIATLGLPNIAFAEENVSELKALTFKAASKSDLALTPENKIIGYNNFYEFGTDKAAPAKFAKDFKTDPWQLEISGEVENPFVLNHQQLFNTFPLEERIYRFRCVEAWSMVVPWIGFELARLVEMAKPSSKAKYVVFHTLYDPEQMPGQKNPLFGGSIDYPYVEALTIEEAMNSLTLLSVGLYGKMLPPQNGAPIRLVMPWKYGFKSIKSIVKISFSETRPKTTWESLAPTEYGFYANVNPNVDHPRWSQGSERVIGAGGLLSVKRQPTLMFNGYEDQVAHLYKDLDLKVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
317 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.746 kDa
Sequence
MNKFTKTDVTPEKLFIQRRKIIQGMSVLSAAAAFPNLAAAKKTEEKRTALSFKADNKPDLILTPENKVIGYNNYYEFGVDKASPAKFASTLKTEPWTIEVSGEVENPMIFTLAQLLAFPLEERIYRLRCVEAWSMIVPWIGFELSRLLEKAKPTGKAKYVAFETLYDPANMPGQKNTLFGGGLDYPYKEGLTLAEAMNPLTILSVGLYGKTLTPQNGAPIRLVVPWKYGFKSIKSIVKIRLTERQPVTTWNQLTPHEYGFYANVNPEVDHPRWSQASERIIGSGGLFTVKRQPTLPFNGYEKEVAHLYKGLDLKVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Haemophilus somnus (strain 129Pt)
Length
317 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.141 kDa
Sequence
MKKLISNDVTPEEIFYQRRKIIKAFGLSAVATALPTFSFAQESSDLKALEYKKSTESTLILTPENKVTGYNNFYEFGVDKGSPAHYAKNFQVNPWKLDIGGEVENPFTLNYDQLFTQFPLEERIYRFRCVEAWAMVVPWIGFELNKLLEKAKPTSKAKYVVFHTLYDPEQMPGQKNHFFGGGIHYPYVEALTLAEAMHSLTLMSVGLYGKALAPQNGAPIRLVVPWKYGFKSIKSIVKITLSETRPRTTWESLAPNEYGFYANVNPKVDHPRWSQASERVIGAGGLLSVKRQPTLMFNGYEREVAHLYKGLDLRINY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Histophilus somni (strain 2336)
Length
317 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
36.226 kDa
Sequence
MKKLTSNDVTPEEIFYQRRKIIKAFGLSAVATALPTFSFAQESSDLKALEYKKSTESTLILTPENKVTGYNNFYEFGVDKGSPAHYAKKFQVNPWKLEIGGEVENPFTLNYDQLFTQFPLEERIYRFRCVEAWAMVVPWIGFELNKLLEKAKPTSKAKYVVFHTLYDPEQMPGQKNHFFGGGIHYPYVEALTLAEAMHSLTLMSVGLYGKALAPQNGAPIRLVVPWKYGFKSIKSIVKITLSETRPRTTWESLAPNEYGFYANVNPKVDHPRWSQASERVIGAGGLLRVKRQPTLMFNGYEREVAHLYKGLDLRINY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Rhizobium etli (strain CIAT 652)
Length
315 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.137 kDa
Sequence
MPSYRPPKIASSEITPRRIYMRRREFLGAAALGAVALYGAGKASAAALPAVESKYKLDEKPTPLKDVTTYNNFYEFGLDKGDPAANSGAFKPLPWTVKVDGMVNKPGTFDLEALMKEFPIEERTYRMRCVEAWSMVIPWDGFPLASLLDKVEPLGSAKYVAFETIVRPEEMPGQKGFFQSLDWPYVEGLRLDEARHPLTLLAVGLYGETLANQNGAPIRLVVPWKYGFKGIKSIVRITLTDQQPKNTWQVTNPQEYGFYANVNPAVDHPRWSQASERRIGEGGFFGASRHPTLPFNGYADEVASLYAGMDLKANF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
315 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.119 kDa
Sequence
MPSYRPPKIASSEITPRQVYLRRREFLGAATLGAMALYGAGKASAAAFSAVESKYKVDEKTTPIKDVTTYNNFYEFGLDKGDPAALSGEFKPLPWAVKVDGMVNKPGTFDVEALIKEFPIEERTYRMRCVEAWSMVIPWNGFPLAALLNKVEPLGSAKYVAFETVVRPEEMPGQKGFFQSLDWPYVEGLRLDEARHPLTLLAVGLYGETLPNQNGAPIRLVVPWKYGFKGIKSIVRITLTDQQPKNTWQVTNPQEYGFYANVNPAVDHPRWSQASERRIGGSGFFGASRRPTLPFNGYADEVASLYAGMDLKANF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
313 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.992 kDa
Sequence
MPAYRPPHIASSEITPKSFYLSRRNFLGTAAGLAAIGLAGREAIAAPLSAKPGAYKLDEKLTPLDAVTSYNNFYEFGVGKSDPKENSGKFKPTPWTVKVDGLVSKPQEFGIEELMKYPLEERTYRMRCVEGWSMVIPWIGFPLSALLDKVEPLGSAKYVSFETVVRPEEMPGQSGLFQPLSWPYVEGLRLDEARHPLTILAVGLYGETLPNQNGAPIRLVVPWKYGFKGIKSIMRISLVEKQPETTWKNSNAREYGFYSNVNPHVDHPRWSQATEQRIGEGGFFGTQNRPTLMFNGYDDVASLYTGLDLKANY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Length
313 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.282 kDa
Sequence
MARWRPDMAEREATPEALYLRRRDFLALGAAGAVGLLLPRGARAGDPTGAALQVARKVDQAGGETPTPWDSVTGYNNFYELGTSKEDPSRNAGSLRARPWTVTIAGEVKRPQTLDVDALVRMFPPEERVYRMRCVEAWSMVIPWVGFPLADLVRRLEPTSRAKYVAFQTLLDRDQLPGQRRPVLPWPYVEALRIDEANHPLALLAVGLYGRVLPGQNGAPLRLVVPWKYGFKGAKSIVRITFLADRPHTTWNDAAPDEYGFYANVNPEVDHPRWSQARERRIGEFFRRKTLPFNGYAAEVAPLYAGLDLRKNY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Length
313 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.245 kDa
Sequence
MARWRPDTAEREATPEALYLRRREFLALGAAGAVGLLLPRGARAGEPTGAALQVARKVDQAGGETPTPWDSVTGYNNFYELGTSKEDPSRNAGSLRPRPWTVTVAGEVKKPQTLDLDALTRMFPLEERVYRMRCVEAWSMVIPWVGFPLGDLVRRLEPTSRAKYVAFQTLLDRDQLPGQRRPVLPWPYVESLRIDEAAHPLALLAVGLYGRVLPGQNGAPLRLVVPWKYGFKGAKSIVRITFLADRPHTTWNDAAPDEYGFYANVNPEVDHPRWSQARERRIGEFFRRKTLPFNGYAAEVASLYAGLDLRKNY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Anaeromyxobacter sp. (strain K)
Length
313 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.243 kDa
Sequence
MARWRPDMAEREATPEALYLRRREFLALGAAGAVGLLVARGARAGEPSGAALQVARRVDQAGGETPTPWDSVTGYNNFYELGTSKEDPSRNAGSLRARPWTVTIAGEVKRPQTLDVDALVRMFPPEERVYRMRCVEAWSMVIPWVGFPLADLVRRLEPTSRAKYVAFQTLLDRDQLPGQRRPVLPWPYVEALRIDEATHPLALLAVGLYGRALPGQNGAPLRLVVPWKYGFKGAKSIVRITFLADRPHTTWNDAAPDEYGFYANVNPEVDHPRWSQARERRIGEFFRRKTLPFNGYAAEVAPLYAGLDLRKNY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Rhizobium meliloti (strain 1021)
Length
313 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.687 kDa
Sequence
MPSYRAPKIAAAEITPERFFLDRRTFIAAAAGSLALSVPKPSRAAALEASKSTYRADDPATPEKDATTYNNFYEFGTGKGDPAANSANFKPAPWTVKVDGLVGKPREFGLEELLAFPLEERIYRMRCVEAWSMVIPWIGFPLAALLDRVEPLGSAKYVAFETVVRPEEMPGQSGYFQPLEWPYREGLRLDEARHPLTILSVGLYGKTLPNQNGAPIRLVVPWKYGFKGIKSIVRISLTETPPPCTWNLAGPSEYGFYANVNPAVDHPRWSQATENRIGEGGFFGANRRDTLPFNGYAEDVASLYAGMDLRVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Sinorhizobium fredii (strain NBRC 101917 / NGR234)
Length
312 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.466 kDa
Sequence
MPVYRPPRIAASEITPERFFLDRRSFLAAAGGLVLGGTGMAHAAALKTSASPYKVDETLTPEKDVTSYNNFYEFGTGKADPATNSASFKPTPWTVKVDGLVGKPRQFGLDELLALPLEERIYRMRCVEAWSMVIPWVGFPLASLLDKVEPLGSAKYVAFETVVRPEEMPGQAGYFQPLPWPYQEGLRLDEARHPLTILAVGLYGKTLPNQNGAPLRLVVPWKYGFKGIKSIVRISLTETAPPCTWNLAAPDEYGFYANVNPAVDHPRWSQATENRIGEGGFFGSNRRDTLPFNGYADEVAGLYAGMDLRVNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS)
Length
312 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (By similarity). Involved in protection against reactive chlorine species (RCS) generated by chlorite and hypochlorite (PubMed:25968643).
Similarity
Belongs to the MsrP family.
Mass
35.047 kDa
Sequence
MLIRRPPDLLPSEITPEPLARGRRALLKGLGAGAALAGLGLPQISQAGSLGTLRPSPLSSDEKLTPLKSVTGYNNFYEFGTDKEDPARHAPGRLKTRPWTVTVEGEIKRPRTFSIDDLLKLAPLEERIYRMRCVEGWSMVIPWVGFPLAELIRQVEPNGQARFVEFVTLADPQQMPGVRSPLLDWPYVEGLRLDEAQHPLTLLAVGLYGEVLPAQNGAPIRLVVPWKYGFKSAKSIVRIRFVREQPRSTWMKAGPSEYGFYSNVNPAVDHPRWSQATERRIGEFIKRKTLPFNGYADQVAGLYSGMDLRRFF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Gluconobacter oxydans (strain 621H)
Length
312 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.004 kDa
Sequence
MALFRYPRPLPSEITPRDMYLSRRSLIGGAAALGAVSATADAATLQTHPGPYSGNLTPTPHEDVTHYNNFYEFGMGKADPATQSQTFHPLPWTLEITGLVRKPVRLDVEQLLRSPAIEERIYRMRCVEAWSMVIPWDGIPLATLLKDADPDPHATHVAFESIVRPAEMPGQTEALSGIQWPYVEGLRLDEAMNPLTLLALGIYGETLPNQNGAPLRLVVPWKYGFKGIKSIQRIRLLDHEPPTTWNRLAPDEYGFYANVNPQVDHPRWSQATERVIGARSLFGATRQPTLMFNGYGEQVADLYRGMDLRKNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
Length
311 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.143 kDa
Sequence
MKPKPSDVTPKELFDQRRSFLKLGAASVVATGSVSNLLAALKTKAPSPLSFIPSENLENLKPNSFEQASGYVNFYEFSTSKTAPVGLSKTLRPYPWELLASGEVENPQSLSIDELYQFPLEERIYRFRCVEGWSMVVPWIGFPLSALLERLKPTTKARYVKFTTLLDPTQFPDQKRGALGVIPHPYVEGLRLDEAMHPLTLLAVGMYGEKLPAQNGAPLRLIVPWKYGFKSIKSIAKIELTQEEPLNTWKLLNPREYGFYANVNPEVDHPRWSQASERLLGSLLKQKTLKFNGYEKEVASLYAGMDLKRDF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
310 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
35.511 kDa
Sequence
MRKTSSPRIAPSEITPRDLYHDRRRFMQAAAGAAAAALWPHWLSAGEKLPGVRKTDHVLPDALTPFEDVAHYNNFYEFGTDKETPSRTAGSLKTRPWTVSVEGEVQKPKLFDVDDLLKLAPLEERIYRLRCVEGWSMVVPWVGFPLAELIKRVEPTGNAKFVEFITLYDPARMPGQKSSVLDWPYREALRLDEAMHPLTLLVFGLYGEVLPNQNGAPVRVVVPWKYGFKSAKSIVRIRFVEQQPVSTWTRAVPSEYGFYANVNPQVDHPRWSQAKERRLGEFFKRPTLMFNGYAEQVAHLYAGMDLKKFF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Length
308 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.504 kDa
Sequence
MLIRSAADLRESEVTDKALWLDRRRFLALGAAGALALSGLPAEAGLNTVKGPFSTDEPPTPRKDVTTYNNFYELGVEKSDPAQLAPSYFTKTRPWSVTIAGECAKPGTLGYEDLIKPHRLEDRIYRMRCVEAWSMVIPWVGIPLGEVLKRFEPGSKAKFVEFTTLQDPERLPGQRRSVIDWPYVEGLRIDEAMHPLALLAVGLYGEELLPQNGAPIRLVVPWKYGFKSIKSIVAIRFAETPSRTAWMKAAPREYGFYANVNPAVDHPRWSQGAERRIGEFLKRKTLPFNGYADQVASLYSGMDLAANF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Caulobacter sp. (strain K31)
Length
306 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.462 kDa
Sequence
MLIRHAPDLTDNDVTGHGLYLRRRDFIGGAAGLGLMAAAGSASARGLTYGPGFSTTEAPTPKKDITSYNNFYEFGVNKEDPSENAGSLKTRPWTVRVDGECEKPATFAIDDLIKGNKLEERIYRMRCVEGWSMVIPWVGFPLKDLIAQVKPTSKAKFVAFETLMRPSEMPGQRWDTLQWPYREGLRIDEAVHPLAILAVGLYGDVLPNQNGAPLRLVVPWKYGFKGIKSIVRISLVETMPATAWNVLAPREYGFYSNVNPAVDHPRWSQATERRIGEFRRRETLPFNGYGQYVADLYRGMDLKRNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
306 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.689 kDa
Sequence
MLIRHAPDLTDNDVTDHSLYLKRRTLMAGVAGLGVAGASASHAQAGLTFSRGFSTTEKPTSKEDITTYNNFYEFGVDKSDPAENSGKFKPRPWTVRIDGACEAPRTVGIEDLIGKNKLEERIYRMRCVEGWSMVIPWVGFPLKDLLASVKPTSKAKFVAFETVMRPSEMPGQAWNTLDWPYREGLRIDEAMHPLTLMAVGLYGDVLPNQNGAPLRLVVPWKYGFKGIKSIVRISLVEKQPVTSWNVLAPREYGFYSNVNPAVDHPRWSQATERRIGEFRRRETLAFNGYGEWVADMYRSMDLKRFY

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
305 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.708 kDa
Sequence
MLIRKPADHLPSEITSESVYFNRRQFMAGAAGLLLSAETLAGLAAKKSPLSQLAANDKPNSLKDITSYNNFYEFGTDKSDPAENAHTLRARPWSVLVDGEVAKPRRFSIEELLKFPLEERVYRLRCVEGWSMVIPWVGFPLASLIKQMNPTSRAKYVAFETLQRPSEMPGQRQAVLDWPYREGLRIDEVMHPLAILAVGLYGNALPNQNGAPIRLVVPWKYGFKSIKSIVRIRLQETMPATSWNMANAHEYGFYSNVNPDVDHPRWSQASERRIGEFFKRKTLPFNGYAEQVAGLYRGMDLRKNF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
299 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
33.998 kDa
Sequence
MAHRWINDLTPADITPRGAWMNRRQVMAGMAGAGLAAFAGSAQAETLEPNSWEEITSYNNFYEFGTGKDDPAAYAHLLKTVPWSIKIDGMVERPGDYDFQDILSEMTIEERIYRFRCVEAWSMVIPWNGFELADLLAMAGVQEGAKYVAFETLYRPEEMPGTRYPVLEWPYREGLRLDEAMHPLTLMATGIYGKPLPNQNGAPLRLVVPWKYGFKSIKSIVRITLTDREPPASWNMAIPNEYGFYSNVNPEVNHPRWSQASERRIGGGLFAKRQPTLMFNGYEKEVAGLYQGMDLAKYF

Gene
msrP
Protein
Protein-methionine-sulfoxide reductase catalytic subunit MsrP
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Length
297 amino acids
Function
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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Similarity
Belongs to the MsrP family.
Mass
34.287 kDa
Sequence
MLITPEKLYKQRRNFLKLGAGALISSSVLASKLSALNFTSDTNPNKLEISDEELATNYVNFYEFSTDKRKAVSLAQNFNTQNWKIDISGEIEKPLTLSMEDILKFPLEERIYRFRCVETWSMVVPWVGFELRRLIEMAKPTSEAKFVKFTTLLDKSQFPDQDALFPTIDYPYVEGLRMDEAMHPLTLLAVGMYKKALKPQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQPKSTWESYAPSEYGFYANVNPNVSHPRWSQANERALGDFFTKPTLMFNGYEKEVASLYKNMDLKVNF