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Database: UniProt
Entry: S4XLA4_SORCE
LinkDB: S4XLA4_SORCE
Original site: S4XLA4_SORCE 
ID   S4XLA4_SORCE            Unreviewed;       460 AA.
AC   S4XLA4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 23.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SCE1572_26725 {ECO:0000313|EMBL:AGP32555.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32555.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP32555.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32555.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an
RT   alkaline milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP32555.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGP32555; AGP32555; SCE1572_26725.
DR   KEGG; scu:SCE1572_26725; -.
DR   PATRIC; fig|1254432.3.peg.6046; -.
DR   KO; K01267; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; SCEL1254432:G13DY-5306-MONOMER; -.
DR   Proteomes; UP000014803; 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   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|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AGP32555.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014803};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014803};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   460 AA;  48712 MW;  B8459CCF0E540041 CRC64;
     MTTPEILDRP GDPKPSTDLG ERFAKSADEM SALRERGALA ARDLCAFIDR SPTPYHAVRE
     VASRLAAAGF SELGERDAWA IAPGDRRYVI RGGSTIVAFV AGAEHPAVGG FRVIGAHTDS
     PNLRVKPSAE LSRSGYQQLG VEVYGGVLYS TWLDRDLSVA GRVHIRRDGR VERHLVDLGR
     PVARVPNLAI HLNRGVNSEG LVLNAQKHLA PVIGLGREAD LSALLARAVD APRDAVLGFD
     LCLYDTLRAS IGGLADEFIF ASRLDNLASC HAATAALIGA GAPGAATRVI ALYDHEECGS
     RSAVGAAGSV LRDVLARIVD TFPAREPQAF ARAMAGSLLV SADMAHAVHP NYADQHEPRH
     APQVNRGLVI KSNANQSYAT DGATAAELEA HCHDAGYAPQ RFVVRSDLPC GSTIGPITAA
     ALGMATVDVG APMLSMHSCR EMAGTLDVHL AIETYRRALT
//
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