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Database: UniProt/TrEMBL
Entry: D3RKB3_KLEVT
LinkDB: D3RKB3_KLEVT
Original site: D3RKB3_KLEVT 
ID   D3RKB3_KLEVT            Unreviewed;       428 AA.
AC   D3RKB3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   11-JUN-2014, entry version 28.
DE   RecName: Full=Peptidase B;
DE            EC=3.4.11.23;
DE   AltName: Full=Aminopeptidase B;
GN   Name=pepB; OrderedLocusNames=Kvar_1204;
OS   Klebsiella variicola (strain At-22).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=640131;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-22;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Pinto A.,
RA   Currie C., Woyke T.;
RT   "Complete sequence of Klebsiella variicola At-22.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP001891; ADC57132.1; -; Genomic_DNA.
DR   RefSeq; YP_003438144.1; NC_013850.1.
DR   ProteinModelPortal; D3RKB3; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; ADC57132; ADC57132; Kvar_1204.
DR   GeneID; 8781342; -.
DR   KEGG; kva:Kvar_1204; -.
DR   PATRIC; 32222506; VBIKleVar54872_1215.
DR   HOGENOM; HOG000243130; -.
DR   KO; K07751; -.
DR   OMA; WGEKATL; -.
DR   BioCyc; KVAR640131:GHXG-1230-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   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   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   ACT_SITE    207    207       By similarity{EA3}.
FT   ACT_SITE    281    281       By similarity{EA3}.
FT   METAL       195    195       Manganese 2 (By similarity){EA3}.
FT   METAL       200    200       Manganese 1 (By similarity){EA3}.
FT   METAL       200    200       Manganese 2 (By similarity){EA3}.
FT   METAL       218    218       Manganese 2 (By similarity){EA3}.
FT   METAL       277    277       Manganese 1 (By similarity){EA3}.
FT   METAL       279    279       Manganese 1 (By similarity){EA3}.
FT   METAL       279    279       Manganese 2 (By similarity){EA3}.
SQ   SEQUENCE   428 AA;  46188 MW;  1C98D7B39C35CB1D CRC64;
     MTEAMKITLS TQPADARWGE KASYSINNDG IALHLNGKDD LGLIQRAARK IDGMGIKHVA
     LSGEGWDTDR AWAFWAGYKG PKGTRKVEWP TLDDAQRSEL DNRLTIIDWV RDTINAPAEE
     LGPEQLAQRA VDLLCSVAGE QMSYRITKGE DLREQGYLGL HTVGRGSERP PVLLALDYNP
     TGDKEAPVYA CLVGKGITFD SGGYSIKQSA FMDSMKSDMG GAATITGALA FAITRGLNKR
     VKLYLCCADN LISGNAFKLG DIIHYRNGKT VEVMNTDAEG RLVLADGLID ASAQKPALII
     DAATLTGAAK TALGNDYHAL FSFDDALANR LLASAQAENE AFWRLPLAEF HRNQLPSNFA
     ELNNTGSAAY PAGASTAAGF LSHFVENYHQ GWLHIDCSAT YRKSAVEQWS AGATGLGVRT
     IANLLTAE
//
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