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Database: UniProt
Entry: L7F294_9ACTN
LinkDB: L7F294_9ACTN
Original site: L7F294_9ACTN 
ID   L7F294_9ACTN            Unreviewed;       432 AA.
AC   L7F294;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 28.
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   ORFNames=STRTUCAR8_05466 {ECO:0000313|EMBL:ELP65274.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP65274.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP65274.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP65274.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity
RT   island that shares virulence genes with other actinobacterial plant
RT   pathogens.";
RL   Plasmid 65:118-124(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ELP65274.1}.
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DR   EMBL; AEJB01000397; ELP65274.1; -; Genomic_DNA.
DR   RefSeq; WP_006379679.1; NZ_AEJB01000397.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ELP65274; ELP65274; STRTUCAR8_05466.
DR   PATRIC; fig|698760.3.peg.5910; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000010931; Unassembled WGS sequence.
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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ELP65274.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010931};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
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, ECO:0000313|EMBL:ELP65274.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ELP65274.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       408    408       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   432 AA;  46151 MW;  89BF8E62883BD5D1 CRC64;
     MSAPHRFDRG HTDDLMSFLA ASPSPYHAVA NTAQRLEKAG FRQVAETDSW DGTSGGKYVL
     RGGAIVAWYV PEGAAPHTPF RIVGAHTDSP NLRVKPVPDL GGHGWRQVAV EIYGGPLLNS
     WLDRDLGLAG RLTLRDGTTR LVDVDRPLLR VPQLAIHLDR AVNTDGLKLD KQRHLQPIWG
     MSDDVREGDL IAFVEEECGL APGEVTGWDL MAHSVEPPAY LGRDRELVAG PRMDNLLSVH
     AATAALAAVS TGSGQLPYIP VLAAFDHEEN GSQSDTGADG PLLGSVLERS VFARGGVYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVNGGPI LKVNVNNRYA TDGSGRAVWA
     ATCEKAGVPF QNFVSNNSMP CGTTIGPITA ARHGIKTVDI GVAILSMHSA RELCGADDPH
     LLANALVAFL EG
//
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