ID   PEPB_PASMU              Reviewed;         434 AA.
AC   Q9CM16;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=PM1029;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03113.1; -; Genomic_DNA.
DR   RefSeq; WP_005757139.1; NC_002663.1.
DR   AlphaFoldDB; Q9CM16; -.
DR   SMR; Q9CM16; -.
DR   STRING; 747.DR93_940; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; AAK03113; AAK03113; PM1029.
DR   KEGG; pmu:PM1029; -.
DR   PATRIC; fig|272843.6.peg.1042; -.
DR   HOGENOM; CLU_013734_7_1_6; -.
DR   OMA; HFDIYGW; -.
DR   Proteomes; UP000000809; 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;
KW   Reference proteome.
FT   CHAIN           1..434
FT                   /note="Peptidase B"
FT                   /id="PRO_0000165838"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         221
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
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         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
SQ   SEQUENCE   434 AA;  46877 MW;  170A5FEA25AB9FB2 CRC64;
     MPMQIMLSTQ VADEAWGKNA LLSFHQAQAT IHVTDYSARN TVQKAARKLR GQGIKDVVLA
     GENWDLETCW AFYQGFYSAK QDYAVEFPTL DDAPQAELLA RIQCGDFVRE MINLPAEVIT
     PVELARRAAH FIEEQAEEYG DKSAVSFNII SGEELKAQNY QGIWNVGRGS ANPPAMLQLD
     FNPTGNPDAP VLACLVGKGI TFDSGGYSIK PSDNMSTMRT DMGGAALLTG SLGLAIARGL
     TQRVKLYLCC AENLVSSNAF KLGDIITYSN GVTAEILNTD AEGRLVLADG LIEADKQQPK
     MIIDCATLTG AAKMAVGNDY HSVLSMDDAL VAALFKSAET EQEPFWRLPF AELHRSQIST
     AFADIANTGT VPVGAGASTA TAFLSYFVKN YQQHWLHIDC SATYRKTASD LWAVGATGIG
     VQTLANLLLN PVKG