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Database: UniProt
Entry: A0A0H3J8E9_CLOPA
LinkDB: A0A0H3J8E9_CLOPA
Original site: A0A0H3J8E9_CLOPA 
ID   A0A0H3J8E9_CLOPA        Unreviewed;       435 AA.
AC   A0A0H3J8E9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-NOV-2017, entry version 17.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467,
GN   ECO:0000313|EMBL:AJA51313.1};
GN   ORFNames=CLPA_c12250 {ECO:0000313|EMBL:AJA51313.1};
OS   Clostridium pasteurianum DSM 525 = ATCC 6013.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51313.1, ECO:0000313|Proteomes:UP000030905};
RN   [1] {ECO:0000313|EMBL:AJA51313.1, ECO:0000313|Proteomes:UP000030905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 525 / ATCC 6013 {ECO:0000313|Proteomes:UP000030905};
RX   PubMed=25700415;
RA   Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT   "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT   Clostridium pasteurianum DSM 525.";
RL   Genome Announc. 3:e01591-14(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP009268; AJA51313.1; -; Genomic_DNA.
DR   RefSeq; WP_003446055.1; NZ_JPGY02000001.1.
DR   EnsemblBacteria; AJA51313; AJA51313; CLPA_c12250.
DR   EnsemblBacteria; KRU12679; KRU12679; CP6013_01927.
DR   KEGG; cpae:CPAST_c12250; -.
DR   KEGG; cpat:CLPA_c12250; -.
DR   PATRIC; fig|1262449.3.peg.2643; -.
DR   KO; K01267; -.
DR   Proteomes; UP000030905; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:AJA51313.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030905};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:AJA51313.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030905};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        84     84       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       161    161       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       409    409       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   435 AA;  48529 MW;  85F70B021291AD3C CRC64;
     MNTEIELAKD LIDFIYESPS SFHTVKNIKK ILIKKGFTEL NEGERWELQK GEKYFVIRND
     SAIIAFNIGN GIIAKKGFKI IGAHTDSPSF RIKPSPEMAV EKSYIKLNTE VYGGPILNTW
     LDRPLSVAGR ITVKGKGILY PEAALVNIKR PIMIIPNLAI HMNRSINKGV ELNRQLDVLP
     LLGLINDTLE KDNLLVKTIA REFNIEPEEI LDFDLFLYEY NKGNIIGLNN EFISSSRLDD
     LEMIHASLAA FTEADITDAT NVLACFDNEE IGSSTKQGAD SEFLAGTLER IVISFGGDRE
     DYFRALYKSF MISADAAHAV HPNRGEKSDP TNRPIINKGP VIKISANQKY TSDSNTISVY
     EAICKKAKVP VQKFVNRSDE LGGSTIGPIS STHVGIRTVD MGTPLLAMHS IRELCGVQDH
     IYVKRSLKEF YNENS
//
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