PEPB_VIBCH
ID PEPB_VIBCH Reviewed; 429 AA.
AC Q9KTX5;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Peptidase B {ECO:0000255|HAMAP-Rule:MF_00504};
DE EC=3.4.11.23 {ECO:0000255|HAMAP-Rule:MF_00504};
DE AltName: Full=Aminopeptidase B {ECO:0000255|HAMAP-Rule:MF_00504};
GN Name=pepB {ECO:0000255|HAMAP-Rule:MF_00504}; OrderedLocusNames=VC_0755;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Probably plays an important role in intracellular peptide
CC degradation. {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa, from a peptide or
CC arylamide. Xaa is preferably Glu or Asp but may be other amino acids,
CC including Leu, Met, His, Cys and Gln.; EC=3.4.11.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC Rule:MF_00504}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93920.1; ALT_INIT; Genomic_DNA.
DR PIR; B82283; B82283.
DR RefSeq; NP_230404.2; NC_002505.1.
DR RefSeq; WP_000107237.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KTX5; -.
DR SMR; Q9KTX5; -.
DR STRING; 243277.VC_0755; -.
DR MEROPS; M17.004; -.
DR DNASU; 2615764; -.
DR EnsemblBacteria; AAF93920; AAF93920; VC_0755.
DR GeneID; 57739465; -.
DR KEGG; vch:VC_0755; -.
DR PATRIC; fig|243277.26.peg.719; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_7_1_6; -.
DR OMA; HFDIYGW; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR HAMAP; MF_00504; Aminopeptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..429
FT /note="Peptidase B"
FT /id="PRO_0000165847"
FT ACT_SITE 207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT ACT_SITE 281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
SQ SEQUENCE 429 AA; 46759 MW; 88E908D3D1382449 CRC64;
MSTQMSVFLS TQAAQPQWGE KALISFAEQG ATIHLQQTQD FSAIQRAARK LDNQGIRTAF
LAGEGWDLES IWAFYQGYRD AKKRNTVEWK ALAAAEQVEL EARIKATDWT RDIINKSAEE
VAPRQLATMA AEFIKSLAPD HVSYRIVKDK DLLTEGWEGI YAVGRGSERT SAMLQLDYNP
TGDENAPVFA CLVGKGITFD SGGYSLKPSN MMSAMKADMG GSGMITGALG LAIMRGFNKR
VKLILCCAEN MVSGRALKLG DIITYKNGKT VEIMNTDAEG RLVLADGLIY ASEQKPQLII
DCATLTGAAK NALGNDYHAL LSYDESLSQQ ALAAAKEENE ALWALPLAEF HREMLPSNFA
DLSNISNGDY TPGASTAAAF LSYFVEGYQK GWLHFDCSAT YRKSASDKWA AGATGMGVKM
LARILMQQA
