ID A5L5L2_VIBBS Unreviewed; 431 AA.
AC A5L5L2;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
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 ORFNames=VSWAT3_08953 {ECO:0000313|EMBL:EDK26985.1};
OS Vibrionales bacterium (strain SWAT-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales.
OX NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK26985.1, ECO:0000313|Proteomes:UP000004912};
RN [1] {ECO:0000313|EMBL:EDK26985.1, ECO:0000313|Proteomes:UP000004912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK26985.1,
RC ECO:0000313|Proteomes:UP000004912};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (APR-2007) 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:EDK26985.1}.
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DR EMBL; AAZW01000050; EDK26985.1; -; Genomic_DNA.
DR AlphaFoldDB; A5L5L2; -.
DR MEROPS; M17.004; -.
DR Proteomes; UP000004912; 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; 46310 MW; 4ECC862259C9EC97 CRC64;
MSTQMSVFLS QEAAQPQWGA KAILSFSEVG ATIHIGEGHD LGAVQRAGRT LDGQGISFVS
LSGEGWDLES VWAFNQGYRG PKKKNALEWD ALPEADQAEL EARIRATDWT RDIINKTAEE
VAPRQLATMA AEYIKSVAPE GTVKAKIVKD KDLLTEGWEG IYAVGRGSER TSAMLQLDFN
PTGDESAPVF ACLVGKGITF DSGGYSIKPG QFMTAMKADM GGAATITGGL GLAIERGLNK
RIKLILCCAE NMISGRALKL GDIITYKNGK TVEIMNTDAE GRLVLADGLM YASEQNPELI
IDCATLTGAA KNALGNDYHA LMSFDDELAH QALTAANQEK EGLWPLPLAD FHRGMLPSNF
ADLSNISTGD YTPGASTAAA FLSYFVDDYK KGWMHMDCAG TYRKSPSDKW AAGATGMGVR
TLARILIDQA K
//
