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Y5738_STRCO
ID   Y5738_STRCO             Reviewed;         459 AA.
AC   O86835;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Uncharacterized zinc protease SCO5738;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SCO5738; ORFNames=SC9A10.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Val-35 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AL939124; CAA20289.1; -; Genomic_DNA.
DR   PIR; T35838; T35838.
DR   RefSeq; NP_629863.1; NC_003888.3.
DR   RefSeq; WP_003973289.1; NZ_VNID01000024.1.
DR   AlphaFoldDB; O86835; -.
DR   SMR; O86835; -.
DR   STRING; 100226.SCO5738; -.
DR   GeneID; 1101177; -.
DR   KEGG; sco:SCO5738; -.
DR   PATRIC; fig|100226.15.peg.5826; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_11; -.
DR   InParanoid; O86835; -.
DR   OMA; IDVVCDM; -.
DR   PhylomeDB; O86835; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..459
FT                   /note="Uncharacterized zinc protease SCO5738"
FT                   /id="PRO_0000074428"
FT   ACT_SITE        82
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   459 AA;  49671 MW;  8E9CFC166E11700F CRC64;
     MTSRSATATA RTSSEARAVA RTQTLIKGEH GIGTVRRTTL PGGLRIVTET LPSVRSATFG
     IWAHVGSRDE TPALNGATHY LEHLLFKGTR KRSALDISSA IDAVGGEMNA FTAKEYTCYY
     ARVLDTDLPL AIDVVCDMLT GSLIQEEDVD VERGAILEEI AMTEDDPGDC VHDLFAHTMF
     GDNALGRPVL GTVDTVNALT ADRIRRFYRK HYDPTHLVVA AAGNVDHNKV VRQVRAAFEK
     SGALKDPAAQ PLAPRAGRRT VRAAGRVELI GRKTEQAHVI LGMPGLARTD ERRWAMGVLN
     TALGGGMSSR LFQEVREKRG LAYSVYSYTS GFADCGLFGV YAGCRPSQVH DVLKICRDEL
     DHVAEHGLTD DEIGRAVGQL QGSTVLGLED TGALMNRIGK SELCWGEQMS VDDMLARIAS
     VTPDDVRAVA RDVLGRRPSL SVIGPLKDKQ ASRLHDAVA
 
 
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