ID   PCRA_STAES              Reviewed;         729 AA.
AC   Q8CRT9;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=ATP-dependent DNA helicase PcrA;
DE            EC=3.6.4.12;
GN   Name=pcrA; OrderedLocusNames=SE_1590;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05189.1; -; Genomic_DNA.
DR   RefSeq; NP_765145.1; NC_004461.1.
DR   RefSeq; WP_002457083.1; NZ_WBME01000010.1.
DR   AlphaFoldDB; Q8CRT9; -.
DR   SMR; Q8CRT9; -.
DR   STRING; 176280.SE_1590; -.
DR   EnsemblBacteria; AAO05189; AAO05189; SE_1590.
DR   KEGG; sep:SE_1590; -.
DR   PATRIC; fig|176280.10.peg.1554; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   OMA; YQDTNRT; -.
DR   Proteomes; UP000001411; Chromosome.
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..729
FT                   /note="ATP-dependent DNA helicase PcrA"
FT                   /id="PRO_0000102063"
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..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..673
FT                   /note="Polar residues"
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   729 AA;  83812 MW;  1477889E446E1D92 CRC64;
     MNALVKNMNS EQSEAVRTTE GPLLIMAGAG SGKTRVLTHR IAYLLDEKDV SPYNILAITF
     TNKAAKEMKA RVEHLVGEEA QVIWMSTFHS MCVRILRRDA DRIGIERNFT IIDPTDQKSV
     IKDVLKSENI DSKRFEPRMF IGAISNLKNE LKTPEDAQKE ANDFHSQMVA TVYKGYQRQL
     SRNEALDFDD LIMTTINLFE RVPETLEYYQ NKFQYIHVDE YQDTNKAQYT LVKLLANKFK
     NLCVVGDSDQ SIYGWRGADI QNILSFEEDY PEAKTIFLEQ NYRSTKNILN AANEVIKHNS
     ERKPKGLWTA NSGGDKIQYY EAMTERDEAE YVVKEIMKHQ RSGKKYSEMA ILYRTNAQSR
     VLEETFMKSN IPYTMVGGQK FYDRKEIKDL LSYLRVIANS NDDISLQRII NVPKRGIGPS
     SVEKIQTYAL QNNISMFDAL AEVDFIGLSK KVTQECISFY EMIQNLIKEQ EFLEISEIVD
     EVLQKSGYRD MLDREQSIES RSRLENLDEF MSVPKDYEEN TPLEEQSLIN FLTDLSLVAD
     IDEADTQNGV TLMTMHSAKG LEFPIVFIMG MEESLFPHIR AIKSEDDHEM EEERRICYVA
     ITRAEELLYI TNATTRMLFG RSQSNMPSRF LKEIPEDLLD SHTGQKRQTI SPKSQPKRGF
     SKRTTSTKKQ VSSSDWKVGD KVMHKAWGEG MVSNVNEKNG SVELDIIFKS EGPKRLLAQF
     APITKKEDS