PEPB_YERPN
ID PEPB_YERPN Reviewed; 432 AA.
AC Q1CKA2; C4GRJ8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=YPN_1248;
GN ORFNames=YP516_1369;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000305; ABG17578.1; -; Genomic_DNA.
DR EMBL; ACNQ01000008; EEO77689.1; -; Genomic_DNA.
DR RefSeq; WP_002209829.1; NZ_ACNQ01000008.1.
DR AlphaFoldDB; Q1CKA2; -.
DR SMR; Q1CKA2; -.
DR MEROPS; M17.004; -.
DR EnsemblBacteria; ABG17578; ABG17578; YPN_1248.
DR GeneID; 57975846; -.
DR KEGG; ypn:YPN_1248; -.
DR HOGENOM; CLU_013734_7_1_6; -.
DR OMA; EKSWAFW; -.
DR Proteomes; UP000008936; Chromosome.
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:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..432
FT /note="Peptidase B"
FT /id="PRO_0000258501"
FT ACT_SITE 208
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT ACT_SITE 282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
SQ SEQUENCE 432 AA; 46531 MW; 57FDBB6B4DB67F2D CRC64;
MTTEIMQISL SHNPADARWG EKALISTNDQ GVTIHLTSHD QLGGIQRAAR KIDGQGIKQV
KLAGEGWGLE QSWAFWQGFR GPKGQRSVVW AELPANEKTE LEQRLKIIDW VRDTINAPAE
DLGPEQLAKN AIDLLCAVSC DAVSYRITKG EDLREQNYAG IYTVGRGSDR APVLLALDYN
PTGNPDAPVM ACLVGKGITF DSGGYSLKQS AFMDSMKSDM GGAATLTGAL ALAAARGLKE
RVKLYLCCAD NMVSGNAFKL GDIIRYRNGK TVEIMNTDAE GRLVLADGLI DASEQNAPLI
IDAATLTGAA KTALGNDYHA LFSFDDELAQ ALLNSAHSEH ELFWRLPLAE FHRSQLPSNF
AELNNVAGGA YSAGASTAAA FLSHFVKNYQ QGWLHIDCSA TYRKSAVDQW SAGATGLGVR
TVANLLLAQA KQ
