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Database: UniProt
Entry: V6KJH6_STRRC
LinkDB: V6KJH6_STRRC
Original site: V6KJH6_STRRC 
ID   V6KJH6_STRRC            Unreviewed;       432 AA.
AC   V6KJH6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
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=M878_21050 {ECO:0000313|EMBL:EST29149.1};
OS   Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST29149.1, ECO:0000313|Proteomes:UP000017984};
RN   [1] {ECO:0000313|EMBL:EST29149.1, ECO:0000313|Proteomes:UP000017984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS 12.976 {ECO:0000313|EMBL:EST29149.1};
RX   PubMed=24407645;
RA   Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces roseochromogenes subsp.
RT   oscitans DS 12.976, Producer of the Aminocoumarin Antibiotic
RT   Clorobiocin.";
RL   Genome Announc. 2:e01147-13(2014).
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:EST29149.1}.
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DR   EMBL; AWQX01000183; EST29149.1; -; Genomic_DNA.
DR   RefSeq; WP_023548307.1; NZ_CM002285.1.
DR   EnsemblBacteria; EST29149; EST29149; M878_21050.
DR   GeneID; 33109683; -.
DR   PATRIC; fig|1352936.5.peg.4413; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000017984; 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   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:EST29149.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017984};
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};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017984};
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;  45831 MW;  7DAEE1AA5EF131A7 CRC64;
     MSAPARFDRG HTDDLMSFLA ASPSPYHAVA VAAERLEKAG FRQVAETDAW DGSAGGRYVL
     RGGAIIAWYV PEGAEAHTPF HIVGAHTDSP NLRIKPRPDS GAHGWRQVAV EIYGGPLMNS
     WLDRDLGLVG RLSLRDGSTA LVNVDRPLLR VPQLAIHLDR SVSSEGLKLD KQRHLQPVWG
     LGDDVRDGDL IAFLEQEAGL AAGSVTGWDL MTHPVEAPAY LGRDRDLVAG PRMDNLLSVH
     AGVAALAAVA TSGAPLTRIP VLAAFDHEEN GSQSDTGADG PLLGSVLERS VFARGGSYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVNGGPI LKVNVNNRYA TDGSGRAVFA
     AACEKADVPF QSFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSV RELCGADDPF
     LLANALVAFL EG
//
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