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Database: UniProt
Entry: B2TP75_CLOBB
LinkDB: B2TP75_CLOBB
Original site: B2TP75_CLOBB 
ID   B2TP75_CLOBB            Unreviewed;       463 AA.
AC   B2TP75; U4PJ10;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-SEP-2017, entry version 65.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=CLL_A2845 {ECO:0000313|EMBL:ACD23700.1};
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD23700.1, ECO:0000313|Proteomes:UP000001195};
RN   [1] {ECO:0000313|Proteomes:UP000001195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP001056; ACD23700.1; -; Genomic_DNA.
DR   RefSeq; WP_012424503.1; NC_018648.1.
DR   ProteinModelPortal; B2TP75; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ACD23700; ACD23700; CLL_A2845.
DR   GeneID; 19963958; -.
DR   KEGG; cbk:CLL_A2845; -.
DR   PATRIC; fig|935198.13.peg.2805; -.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACD23700.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001195};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACD23700.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   463 AA;  51454 MW;  CE00033872DC903E CRC64;
     MKSEKNNKNV WNKYEEKGVK EIFDFCDGYK NFMSICKTER ECVKEVIKMA EDNGYKNIDD
     IIKNGGALKA GDKVYANNKG KTIALFIIGN ESMEKGLKIL GAHIDSPRLD AKQNPLYEDN
     EMVLLDTHYY GGIKKYQWVT LPLALHGVVV KKDGSIIDIC IGEDENDPVV GVSDLLVHLS
     GDQLLKKGNK VVEGEDLNVL VGSMPLKGEE KDAVKANILK ILKEKYDFEE EDFLSAEIEI
     VPAGKARDYG LDRSMVMAYG HDDRVCSYTS LKAMFDINEC DKTCCCLLVD KEEVGSIGAT
     GMQSKFFENI VAEVLDKVEG FSDIKLRRCL SNSKMLSSDV SAAFDPNYPS VMEKKNSAFF
     GRGMVFNKYT GARGKSGCND ANAEYMAELR RIMEKHDVSI QTAELGKVDA GGGGTIAYIL
     AQYNMEVIDC GVALLNMHAP WELASKADIY ETMRGYRAFL IEA
//
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