ID A0A3A6QU18_9VIBR Unreviewed; 431 AA.
AC A0A3A6QU18;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Peptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
DE EC=3.4.11.23 {ECO:0000256|HAMAP-Rule:MF_00504};
DE AltName: Full=Aminopeptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
GN Name=pepB {ECO:0000256|HAMAP-Rule:MF_00504,
GN ECO:0000313|EMBL:RJX71767.1};
GN ORFNames=DZ860_10420 {ECO:0000313|EMBL:RJX71767.1};
OS Vibrio sinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2302434 {ECO:0000313|EMBL:RJX71767.1, ECO:0000313|Proteomes:UP000273252};
RN [1] {ECO:0000313|EMBL:RJX71767.1, ECO:0000313|Proteomes:UP000273252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEI233 {ECO:0000313|EMBL:RJX71767.1,
RC ECO:0000313|Proteomes:UP000273252};
RA Li Y.;
RT "Vibrio isolated from the Eastern China Marginal Seas.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays an important role in intracellular peptide
CC degradation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00504};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00504};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJX71767.1}.
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DR EMBL; QVMU01000007; RJX71767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A6QU18; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000273252; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00504; Aminopeptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00504};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00504};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00504};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00504};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00504};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00504}.
FT DOMAIN 276..283
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 208
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT ACT_SITE 282
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
SQ SEQUENCE 431 AA; 46578 MW; 4BA4D3BF669FF7CB CRC64;
MSTEMYVFLS QDPAAPVWGK KAILSFSDKG ATIHLGEGHD LGAIQRAARK LDGQGIQSIE
LAGSDWDLES VWAFHQGYRS SKKTNALLWP ELAEDAQFEL KARIKATDFT RDIINKTAEE
VAPRQLATMA AEFIKSVAPK ESVTVRIVKD KDLLSEGWEG IYAVGRGSER TSAMLQLDFN
PTGDKDAPVF ACLVGKGITF DSGGYSLKPS DFMASMKADM GGAGTITGGL ALAIMRGLNK
RVKLILCCAE NMISGRALKL GDIITYKNGK TVEIMNTDAE GRLVLADGLL YASEQNPDLI
IDCATLTGAA KYALGNDYHA VMSFDDELSH QALTVAREEK EGLWPLPLAD FHRSMLPSNF
ADLSNIGSGD YSPGASTAAA FLSYFVDDYK KGWLHFDCAA TYRRAPSDKW SAGATGMGVR
TLAGILTEQA K
//
