ID A0A0F7H607_SERFO Unreviewed; 431 AA.
AC A0A0F7H607;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:VTR61023.1};
GN ORFNames=NCTC12965_08709 {ECO:0000313|EMBL:VTR61023.1}, WN53_00750
GN {ECO:0000313|EMBL:AKG67784.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG67784.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG67784.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG67784.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VTR61023.1, ECO:0000313|Proteomes:UP000358076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12965 {ECO:0000313|EMBL:VTR61023.1,
RC ECO:0000313|Proteomes:UP000358076};
RG Pathogen Informatics;
RL Submitted (MAY-2019) 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}.
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DR EMBL; CP011254; AKG67784.1; -; Genomic_DNA.
DR EMBL; CABEEZ010000167; VTR61023.1; -; Genomic_DNA.
DR RefSeq; WP_024484242.1; NZ_SUPV01000020.1.
DR AlphaFoldDB; A0A0F7H607; -.
DR STRING; 47917.AV650_23475; -.
DR GeneID; 30318678; -.
DR KEGG; sfw:WN53_00750; -.
DR PATRIC; fig|47917.8.peg.159; -.
DR Proteomes; UP000034699; Chromosome.
DR Proteomes; UP000358076; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000034699}.
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; 46614 MW; 2C31867CA1DCA34F CRC64;
MTTEIMQITL SQQPADARWG EKALLSTNDQ GITIHLSNSG KLGLIQRAAR RIDGQGIKKV
KLAGEGWDLE NSWAFWQGYR GPKGQRSVEW AELPEAESQE LQQRLKIVDW VRDTINMPAE
ELGPEQLATR AVDLMCAVGC DAVSYRITKG EDLREQNYAG IHTVGRGSDR SPVLLALDFN
PTGNPEAPVF ACLVGKGITF DSGGYSLKQS AFMDSMKSDM GGAATITGAL ALAVARGLQQ
RVKLYLCCAD NMVSGNAFKL GDIIRYRNGK TVEVMNTDAE GRLVLADGLI DASAQNPELI
IDCATLTGAA KTAVGNDYHA LFSFDDALAQ ELLASADEEH EPFWRLPLAE FHRSQLPSNF
AELNNVAGPA YTAGASTAAA FLSHFVQNYQ KGWLHIDCSA TYRKGAVDQW SAGATGLGVR
TLANLLLSKA K
//
