ID D3RKB3_KLEVT Unreviewed; 428 AA.
AC D3RKB3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 01-MAY-2013, entry version 23.
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; ENEAFWR; -.
DR BioCyc; KVAR640131:GHXG-1229-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA: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 ACT_SITE 207 207 By similarity.
FT ACT_SITE 281 281 By similarity.
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 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
//
