ID   PEPB_ECOSE              Reviewed;         427 AA.
AC   B6I595;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ECSE_2809;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG78333.1; -; Genomic_DNA.
DR   RefSeq; WP_000133582.1; NC_011415.1.
DR   AlphaFoldDB; B6I595; -.
DR   SMR; B6I595; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; BAG78333; BAG78333; ECSE_2809.
DR   GeneID; 66673589; -.
DR   KEGG; ecy:ECSE_2809; -.
DR   HOGENOM; CLU_013734_7_1_6; -.
DR   OMA; EKSWAFW; -.
DR   Proteomes; UP000008199; 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..427
FT                   /note="Peptidase B"
FT                   /id="PRO_1000127008"
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;  46226 MW;  C76F956739134150 CRC64;
     MTEAMKITLS TQPADARWGE KATYSINNDG ITLHLNGADD LGLIQRAARK IDGLGIKHVQ
     LSGEGWDADR CWAFWQGYKA PKGTRKVEWP DLDDAQRQEL DNRLMIIDWV RDTINAPAEE
     LGPSQLAQRA VDLISNVAGD RVTYRITKGE DLREQGYMGL HTVGRGSERS PVLLALDYNP
     TGDKEAPVYA CLVGKGITFD SGGYSIKQTA FMDSMKSDMG GAATVTGALA FAITRGLNKR
     VKLFLCCADN LISGNAFKLG DIITYRNGKK VEVMNTDAEG RLVLADGLID ASAQKPEMII
     DAATLTGAAK TALGNDYHAL FSFDDALAGR LLASASQENE PFWRLPLAEF HRSQLPSNFA
     ELNNTGSAAY PAGASTAAGF LSHFVENYQQ GWLHIDCSAT YRKAPVEQWS AGATGLGVRT
     IANLLTA