bepA

Protein adenylyltransferase

544 amino acids

Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host target proteins.

61.341 kDa

MPKAKAKTKNTEIISPHHYVYPNTTTLKNKYGIKNLNAFLEKCSHDTAKAMINLREESLPEYFDTAYLCHIHQQLFKNTFEWAGYLRHIPFTFADGTTAAMPEMKRTGWKNAFAIGDEIQEGLQRLDQTLAEKNNLQGLTREEFNSEAIELFNSLNQLHPFREGNGRTQRLFFENLAKAAGHQLNFSLITKERMMVASVAVAENGDLEPMQHLFEDISNPEKIRLLKEFMHTMKNTGRNVNDRPVMVAKEGETYTGTYRGAGLEGFALNVKGAYIIGNIDHLPPEQLKILKPGDKITFTAPKAEELKKTLIPKETLVPLTKLEIAEMVAEDAFVHTCRDQICSLSKIVYGSQGVLNKNIIEIIKNPSKGQQLATQIERTPYSVHSLAGFDLICFKTGARVRAEKHVALLSCAVANFTHAVKHARQEITKEHQAEQNRLRQEVPMPSQSLQDLLSLPKEFQQKALGVSPLLQKELTSLLQKVNSRLSSSEQRALRENNHETLAKNLGVSEQKAKEITKTVMKAREVQQKSQTRTVSHSKTLAMAS

bepA

Beta-barrel assembly-enhancing protease

487 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Belongs to the peptidase M48 family. BepA subfamily.

53.935 kDa

MFRQLKKNLVATLIAAMTIGQVAPAFADSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRNAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDARIDQLRQLQERFKPYTKM

bepA

Beta-barrel assembly-enhancing protease

487 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions.

Belongs to the peptidase M48 family. BepA subfamily.

53.908 kDa

MFRQLKKNLVATLIAAMTIGQVAPAFADSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDARIDQLRQLQERFKPYTKM

bepA

Beta-barrel assembly-enhancing protease

487 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Belongs to the peptidase M48 family. BepA subfamily.

53.741 kDa

MFRQLKKNLVATLIAALALGQVAPAFADPADTLPDMGTSAGSTLSIGQEMQMGDFYVRQLRGSAPLINDPLLVQYINALGMRLVSHADSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYADNESQLASVMAHEISHVTQRHLARAMEDQKRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRAGFDPQAMPSFLEKLLDQARYSTRPPEILLTHPLPESRLADARNRANQMRPVVVQSSADFYFAKARALGMYNSGRNQLTSDLLDQWSKGNVRQQHAAQYGRALQAMEASKYDEARKTLQPLLSAEPNNAWYLDLATDIDLGQKRANDAINRLKNARDLRVNPVLQLNLANAYLQGGQPKAAETILNRYTFSHKDDGNGWDLLAQAEAALNNRDQELAARAESYALAGRLDQAISLLSSASAQAKLGSQQQARYDARIDQLRQLQERFKPYTKM

bepA

Beta-barrel assembly-enhancing protease

487 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Belongs to the peptidase M48 family. BepA subfamily.

53.741 kDa

MFRQLKKNLVATLIAALALGQVAPAFADPADTLPDMGTSAGSTLSIGQEMQMGDFYVRQLRGSAPLINDPLLVQYINALGMRLVSHADSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYADNESQLASVMAHEISHVTQRHLARAMEDQKRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRAGFDPQAMPSFLEKLLDQARYSTRPPEILLTHPLPESRLADARNRANQMRPVVVQSSADFYFAKARALGMYNSGRNQLTSDLLDQWSKGNVRQQHAAQYGRALQAMEASKYDEARKTLQPLLSAEPNNAWYLDLATDIDLGQKRANDAINRLKNARDLRVNPVLQLNLANAYLQGGQPKAAETILNRYTFSHKDDGNGWDLLAQAEAALNNRDQELAARAESYALAGRLDQAISLLSSASAQAKLGSQQQARYDARIDQLRQLQERFKPYTKM

bepA

Beta-barrel assembly-enhancing protease

487 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Belongs to the peptidase M48 family. BepA subfamily.

53.908 kDa

MFRQLKKNLVATLIAAMTIGQVAPAFADSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDARIDQLRQLQERFKPYTKM

bepA

Beta-barrel assembly-enhancing protease

486 amino acids

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Belongs to the peptidase M48 family. BepA subfamily.

53.418 kDa

MIATLLSSLLLTGPISAGAETQGLLPAQDLLPDIGTSAGATLSIDQEMAMGDFYVRQMRASAPLIYDPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHLARAMEEQQRLAPLTWVGVLGSILLTMASPQAGMAGLSGTLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRYVSKPPEMLLTHPLPDSRLSDARNRANQMKPHPTASSQDYLFAKMRILGMYGADENSLTPELLDKLSKGTVREQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDASARVKLGSLEQARYDARIDQLRRLNERFRKYQKS