PCRA_BACSU
ID PCRA_BACSU Reviewed; 739 AA.
AC O34580;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-dependent DNA helicase PcrA;
DE EC=3.6.4.12;
GN Name=pcrA; Synonyms=yerF; OrderedLocusNames=BSU06610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9701819; DOI=10.1046/j.1365-2958.1998.00927.x;
RA Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D.,
RA Bruand C.;
RT "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling
RT functions both in repair and rolling-circle replication.";
RL Mol. Microbiol. 29:261-273(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INTERACTION WITH YXAL; YWHK AND YERB.
RX PubMed=12073041; DOI=10.1007/s00438-002-0670-9;
RA Noirot-Gros M.-F., Soultanas P., Wigley D.B., Ehrlich S.D., Noirot P.,
RA Petit M.-A.;
RT "The beta-propeller protein YxaL increases the processivity of the PcrA
RT helicase.";
RL Mol. Genet. Genomics 267:391-400(2002).
RN [4]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
CC -!- FUNCTION: DNA helicase used for plasmid rolling-circle replication and
CC also involved in UV repair.
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 -!- SUBUNIT: Interacts with YxaL; YwhK and YerB. Interacts with the RNA
CC polymerase core (PubMed:21710567). {ECO:0000269|PubMed:12073041,
CC ECO:0000269|PubMed:21710567}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y15254; CAA75552.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12481.1; -; Genomic_DNA.
DR PIR; E69794; E69794.
DR RefSeq; NP_388543.1; NC_000964.3.
DR RefSeq; WP_003233919.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O34580; -.
DR SMR; O34580; -.
DR IntAct; O34580; 5.
DR STRING; 224308.BSU06610; -.
DR PaxDb; O34580; -.
DR EnsemblBacteria; CAB12481; CAB12481; BSU_06610.
DR GeneID; 938747; -.
DR KEGG; bsu:BSU06610; -.
DR PATRIC; fig|224308.179.peg.719; -.
DR eggNOG; COG0210; Bacteria.
DR InParanoid; O34580; -.
DR OMA; YQDTNRT; -.
DR PhylomeDB; O34580; -.
DR BioCyc; BSUB:BSU06610-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..739
FT /note="ATP-dependent DNA helicase PcrA"
FT /id="PRO_0000102051"
FT DOMAIN 10..289
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 290..570
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT REGION 655..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 739 AA; 83555 MW; 70C553EFC88E6D6D CRC64;
MNYISNQLLS GLNPVQQEAV KTTDGPLLLM AGAGSGKTRV LTHRIAYLMA EKHVAPWNIL
AITFTNKAAR EMKERVESIL GPGADDIWIS TFHSMCVRIL RRDIDRIGIN RNFSILDTAD
QLSVIKGILK ERNLDPKKFD PRSILGTISS AKNELTEPEE FSKVAGGYYD QVVSDVYADY
QKKLLKNQSL DFDDLIMTTI KLFDRVPEVL EFYQRKFQYI HVDEYQDTNR AQYMLVKQLA
ERFQNLCVVG DSDQSIYRWR GADITNILSF EKDYPNASVI LLEQNYRSTK RILRAANEVI
KNNSNRKPKN LWTENDEGIK ISYYRGDNEF GEGQFVAGKI HQLHSTGKRK LSDIAILYRT
NAQSRVIEET LLKAGLNYNI VGGTKFYDRK EIKDILAYLR LVSNPDDDIS FTRIVNVPKR
GVGATSLEKI ASYAAINGLS FFQAIQQVDF IGVSAKAANA LDSFRQMIEN LTNMQDYLSI
TELTEEILDK TEYREMLKAE KSIEAQSRLE NIDEFLSVTK NFEQKSEDKT LVAFLTDLAL
IADIDQLDQK EEESGGKDAI TLMTLHAAKG LEFPVVFLMG LEEGVFPHSR SLMEEAEMEE
ERRLAYVGIT RAEQELYLTN AKMRTLFGRT NMNPESRFIA EIPDDLLENL NEKKETRATS
ARKMQPRRGP VSRPVSYASK TGGDTLNWAV GDKAGHKKWG TGTVVSVKGE GEGTELDIAF
PSPVGVKRLL AAFAPIEKQ