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Database: UniProt
Entry: B5GU75_STRC2
LinkDB: B5GU75_STRC2
Original site: B5GU75_STRC2 
ID   B5GU75_STRC2            Unreviewed;       436 AA.
AC   B5GU75;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   25-OCT-2017, entry version 57.
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=SCLAV_3006 {ECO:0000313|EMBL:EFG08077.1}, SSCG_02899
GN   {ECO:0000313|EMBL:EDY49871.1};
OS   Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 /
OS   NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=443255 {ECO:0000313|EMBL:EDY49871.1, ECO:0000313|Proteomes:UP000006569};
RN   [1] {ECO:0000313|EMBL:EDY49871.1, ECO:0000313|Proteomes:UP000006569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 {ECO:0000313|EMBL:EDY49871.1}, and ATCC 27064 / DSM
RC   738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602
RC   {ECO:0000313|Proteomes:UP000006569};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A.,
RA   Heiman D., Hepburn T., Sykes S., Godfrey P., Alvarado L., Kodira C.D.,
RA   Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S.,
RA   Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces clavuligerus ATCC 27064.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFG08077.1, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 {ECO:0000313|EMBL:EFG08077.1}, and ATCC 27064 / DSM
RC   738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602
RC   {ECO:0000313|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C.,
RA   Bovenberg R.A.L., Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
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; DS570646; EDY49871.1; -; Genomic_DNA.
DR   EMBL; CM000913; EFG08077.1; -; Genomic_DNA.
DR   RefSeq; WP_003955381.1; NZ_DS570646.1.
DR   STRING; 443255.SclaA2_010100014364; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EDY49871; EDY49871; SSCG_02899.
DR   EnsemblBacteria; EFG08077; EFG08077; SCLAV_3006.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000002357; Chromosome.
DR   Proteomes; UP000006569; 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   InterPro; IPR023367; Peptidase_M42_dom2.
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:EFG08077.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002357,
KW   ECO:0000313|Proteomes:UP000006569};
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:UP000002357};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        92     92       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       163    163       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       412    412       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   436 AA;  46590 MW;  7E1153DEF62C45E5 CRC64;
     MSTSAPVRFD RGHTDDLMTF LAASPSPYHA VATAAQRLEK AGFRQVRETD AWDTGAGAGT
     GGKYVVRGGA LIAWYVPEGA DPHTPFRIVG AHTDSPNLRV KPDPDTGAHG WRQIAVEIYG
     GALLNSWLDR DLGISGRLSL RDGSHRLVNV DRPLLRVPQL AIHLDRAVNT DGLKLDKQRH
     MQPIWGLGEV HEGDLVHFLA EESGLDANDI VGWDLMTHSV EAPAYLGRDR ELLAAPRLDN
     LLSVHAATAA LAAAARTPDL AYIPVLAAFD HEENGSQADT GADGPLLGSV LERSVFARGG
     TYEDRARAFA STVCLSSDVG HAVHPNYAER HDPTHHPLPN GGPILKVNVN QRYATDGSGR
     AVFAAACERA GSPWQSFVSN NAMPCGTTIG PITAARHGIH TVDIGVACLS MHSVRELCGA
     DDPYLLANVL TAFLQG
//
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