ID   PEPB_CITK8              Reviewed;         427 AA.
AC   A8AD60;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CKO_00258;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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; CP000822; ABV11422.1; -; Genomic_DNA.
DR   RefSeq; WP_012131254.1; NC_009792.1.
DR   AlphaFoldDB; A8AD60; -.
DR   SMR; A8AD60; -.
DR   STRING; 290338.CKO_00258; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; ABV11422; ABV11422; CKO_00258.
DR   GeneID; 45134541; -.
DR   KEGG; cko:CKO_00258; -.
DR   HOGENOM; CLU_013734_7_1_6; -.
DR   OMA; EKSWAFW; -.
DR   OrthoDB; 356206at2; -.
DR   Proteomes; UP000008148; 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..427
FT                   /note="Peptidase B"
FT                   /id="PRO_1000014887"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         277
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
SQ   SEQUENCE   427 AA;  46300 MW;  51E5BE1CD2BCFE50 CRC64;
     MTEAMKITLS TQPADARWGD KATYSINNDG ITLHLNGKDD SGLIQRAARK IDGLGIKHVQ
     LTGAGWDVER SWAFWQGYKG PKGSRKVEWP DLDDEKRKEL DNRLTIIDWV RDTINAPAEE
     LGPEQLAQRA VDLLCSVACD HVSYRITKGE DLREQNYMGL HTVGRGSDRA PVLLALDYNP
     TGDKDAPVYA CLVGKGITFD SGGYSIKQSA FMDSMKSDMG GAATVTGALA FAITRGLNKR
     VKLYLCCADN LISGNAFKLG DIIHYRNGKN VEVMNTDAEG RLVLADGLID ASAQKPELII
     DAATLTGAAK TALGNDYHAL FSFDDALAGR LLASAAEENE PFWRLPLAEF HRNQLPSNFA
     ELNNTGSAAY PAGASTAAGF LSHFVENYQQ GWLHIDCSAT YRKAPVEQWS AGATGLGVRT
     IANLLTA