ID   PEPB_YERP3              Reviewed;         432 AA.
AC   A7FFX8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
GN   OrderedLocusNames=YpsIP31758_1175;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS45791.1; -; Genomic_DNA.
DR   RefSeq; WP_012104798.1; NC_009708.1.
DR   AlphaFoldDB; A7FFX8; -.
DR   SMR; A7FFX8; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; ABS45791; ABS45791; YpsIP31758_1175.
DR   KEGG; ypi:YpsIP31758_1175; -.
DR   HOGENOM; CLU_013734_7_1_6; -.
DR   OMA; EKSWAFW; -.
DR   Proteomes; UP000002412; 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_1000060519"
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;  46518 MW;  9592F70D4B6515AE CRC64;
     MTTEIMQISL SHNPADARWG EKALISTNDQ GVTIHLTSHD QLGGIQRAAR KIDGQGIKQV
     KLAGEGWGLE QSWAFWQGFR GPKGQRSVVW AELPANEKTE LEQRLQIIDW VRDTINAPAE
     DLGPEQLAKN AIDLLCAVSC DAVSYRITKG EDLREQNYAG IYTVGRGSDR APVLLALDYN
     PTGNPDAPVM ACLVGKGITF DSGGYSLKQS AFMDSMKSDM GGAATLTGAL ALAAARGLKE
     RVKLYLCCAD NMVSGNAFKL GDIIRYRNGK TVEIMNTDAE GRLVLADGLI DASEQNAPLI
     IDAATLTGAA KTALGNDYHA LFSFDDELAQ ALLTSAHSEH ELFWRLPLAE FHRSQLPSNF
     AELNNVAGGA YSAGASTAAA FLSHFVKNYQ QGWLHIDCSA TYRKSAVDQW SAGATGLGVR
     TVANLLLAQA KQ