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PCRA_STAAS
ID   PCRA_STAAS              Reviewed;         730 AA.
AC   Q6G828;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=ATP-dependent DNA helicase PcrA;
DE            EC=3.6.4.12;
GN   Name=pcrA; OrderedLocusNames=SAS1828;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Essential helicase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX571857; CAG43633.1; -; Genomic_DNA.
DR   RefSeq; WP_000992921.1; NC_002953.3.
DR   AlphaFoldDB; Q6G828; -.
DR   SMR; Q6G828; -.
DR   KEGG; sas:SAS1828; -.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   OMA; YQDTNRT; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01073; pcrA; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..730
FT                   /note="ATP-dependent DNA helicase PcrA"
FT                   /id="PRO_0000102060"
FT   DOMAIN          6..285
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          286..560
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   REGION          641..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   730 AA;  84074 MW;  3C7D6A9501BC3251 CRC64;
     MNALLNHMNT EQSEAVKTTE GPLLIMAGAG SGKTRVLTHR IAYLLDEKDV SPYNVLAITF
     TNKAAREMKE RVQKLVGDQA EVIWMSTFHS MCVRILRRDA DRIGIERNFT IIDPTDQKSV
     IKDVLKNENI DSKKFEPRMF IGAISNLKNE LKTPADAQKE ATDYHSQMVA TVYSGYQRQL
     SRNEALDFDD LIMTTINLFE RVPEVLEYYQ NKFQYIHVDE YQDTNKAQYT LVKLLASKFK
     NLCVVGDSDQ SIYGWRGADI QNILSFEKDY PEANTIFLEQ NYRSTKTILN AANEVIKNNS
     ERKPKGLWTA NTNGEKIHYY EAMTERDEAE FVIREIMKHQ RNGKKYQDMA ILYRTNAQSR
     VLEETFMKSN MPYTMVGGQK FYDRKEIKDL LSYLRIIANS NDDISLQRII NVPKRGVGPS
     SVEKVQNYAL QNNISMFDAL GEADFIGLSK KVTQECLNFY ELIQSLIKEQ EFLEIHEIVD
     EVLQKSGYRE MLERENTLES RSRLENIDEF MSVPKDYEEN TPLEEQSLIN FLTDLSLVAD
     IDEADTENGV TLMTMHSAKG LEFPIVFIMG MEESLFPHIR AIKSEDDHEM QEERRICYVA
     ITRAEEVLYI THATSRMLFG RPQSNMPSRF LKEIPESLLE NHSSGKRQTI QPKAKPFAKR
     GFSQRTTSTK KQVLSSDWNV GDKVMHKAWG EGMVSNVNEK NGSIELDIIF KSQGPKRLLA
     QFAPIEKKED
 
 
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