ID   PEPB_ECO45              Reviewed;         427 AA.
AC   B7MI07;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   16-OCT-2013, entry version 31.
DE   RecName: Full=Peptidase B;
DE            EC=3.4.11.23;
DE   AltName: Full=Aminopeptidase B;
GN   Name=pepB; OrderedLocusNames=ECS88_2699;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Probably plays an important role in intracellular
CC       peptide degradation (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa, from
CC       a peptide or arylamide. Xaa is preferably Glu or Asp but may be
CC       other amino acids, including Leu, Met, His, Cys and Gln.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928161; CAR03965.1; -; Genomic_DNA.
DR   RefSeq; YP_002392362.1; NC_011742.1.
DR   ProteinModelPortal; B7MI07; -.
DR   SMR; B7MI07; 64-426.
DR   STRING; 585035.ECS88_2699; -.
DR   EnsemblBacteria; CAR03965; CAR03965; ECS88_2699.
DR   GeneID; 7130650; -.
DR   KEGG; ecz:ECS88_2699; -.
DR   PATRIC; 18413104; VBIEscCol91599_2668.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243130; -.
DR   KO; K07751; -.
DR   OMA; NMVSGRA; -.
DR   ProtClustDB; PRK05015; -.
DR   BioCyc; ECOL585035:GJWP-2691-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-HAMAP.
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:SF3; PTHR11963:SF3; 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; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW   Metal-binding; Protease.
FT   CHAIN         1    427       Peptidase B.
FT                                /FTId=PRO_1000127002.
FT   ACT_SITE    207    207       Potential.
FT   ACT_SITE    281    281       Potential.
FT   METAL       195    195       Manganese 2 (By similarity).
FT   METAL       200    200       Manganese 1 (By similarity).
FT   METAL       200    200       Manganese 2 (By similarity).
FT   METAL       218    218       Manganese 2 (By similarity).
FT   METAL       277    277       Manganese 1 (By similarity).
FT   METAL       279    279       Manganese 1 (By similarity).
FT   METAL       279    279       Manganese 2 (By similarity).
SQ   SEQUENCE   427 AA;  46231 MW;  954008AF1FBAD58C CRC64;
     MTEAMKITLS TQPADARWGE KATYSINNDG ITLHLNGADD LGLIQRAARK IDGLGIKHVQ
     LSGEGWDADR CWAFWQGYKA PKGIRKVEWP DLDDAQRQEL DNRLMIIDWV RDTINAPAEE
     LGPSQLAQRA VDLISNVAGD RVTYRITKGE DLREQGYMGL HTVGRGSERS PVLLALDYNP
     TGDKEAPVYA CLVGKGITFD SGGYSIKQTA FMDSMKSDMG GAATVTGALA FAITRGLNKR
     VKLFLCCADN LISGNAFKLG DIITYRNGKK VEVMNTDAEG RLVLADGLID ASAQKPELII
     DAATLTGAAK TALGNDYHAL FSFDDALAGR LLASAAQENE PFWRLPLAEF HRNQLPSNFA
     ELNNTGSAAY PAGASTAAGF LSHFVENYQQ GWLHIDCSAT YRKAPVEQWS AGATGLGVRT
     IANLLTA
//