RECS_BACSU
ID RECS_BACSU Reviewed; 496 AA.
AC P50729;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable ATP-dependent DNA helicase RecS;
DE EC=3.6.4.12;
DE AltName: Full=Recombination protein S;
GN Name=recS; Synonyms=ypbC; OrderedLocusNames=BSU23020;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
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 DISRUPTION PHENOTYPE.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=9642195; DOI=10.1128/jb.180.13.3405-3409.1998;
RA Fernandez S., Sorokin A., Alonso J.C.;
RT "Genetic recombination in Bacillus subtilis 168: effects of recU and recS
RT mutations on DNA repair and homologous recombination.";
RL J. Bacteriol. 180:3405-3409(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006;
RA Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.;
RT "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the
RT absence of DNA end processing.";
RL J. Bacteriol. 188:353-360(2006).
CC -!- FUNCTION: Probable DNA helicase. Required in synaptic and/or post-
CC synaptic stages of recombination. Probably has overlapping function
CC with RecQ (AC O34748). It probably acts to help generate ss-DNA from
CC ds-DNA breaks. {ECO:0000269|PubMed:16385024}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an increased
CC sensitivity to DNA damaging agents, 100-fold decreased plasmid
CC transformation and 4-fold reduced chromosomal DNA transformation.
CC Sensitivity increases in the presence of mutated AddAB nuclease.
CC {ECO:0000269|PubMed:16385024, ECO:0000269|PubMed:9642195}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; L47648; AAC83947.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14218.1; -; Genomic_DNA.
DR PIR; A69691; A69691.
DR RefSeq; NP_390183.1; NC_000964.3.
DR RefSeq; WP_003230528.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50729; -.
DR SMR; P50729; -.
DR STRING; 224308.BSU23020; -.
DR PaxDb; P50729; -.
DR PRIDE; P50729; -.
DR EnsemblBacteria; CAB14218; CAB14218; BSU_23020.
DR GeneID; 938969; -.
DR KEGG; bsu:BSU23020; -.
DR PATRIC; fig|224308.179.peg.2509; -.
DR eggNOG; COG0514; Bacteria.
DR InParanoid; P50729; -.
DR OMA; CRWQFLL; -.
DR PhylomeDB; P50729; -.
DR BioCyc; BSUB:BSU23020-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030894; C:replisome; 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:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..496
FT /note="Probable ATP-dependent DNA helicase RecS"
FT /id="PRO_0000205035"
FT DOMAIN 25..192
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 219..363
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 136..139
FT /note="DEAH box"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 496 AA; 56508 MW; DDC2FED715875F2D CRC64;
MTKLQQTLYQ FFGFTSFKKG QQDIIESILS GKDTIAMLPT GGGKSLCYQL PGYMLDGMVL
IVSPLLSLME DQVQQLKARG EKRAAALNSM LNRQERQFVL EHIHRYKFLY LSPEALQSPY
VLEKLKSVPI SLFVIDEAHC ISEWGHDFRP DYSKLGQLRK KLGHPPVLAL TATATKETLQ
DVMNLLELQH AVRHLNSVNR PNIALRVENA ADTAEKIDRV IQLVENLQGP GIVYCPTRKW
AKELAGEIKS KTSSRADFYH GGLESGDRIL IQQQFIHNQL DVICCTNAFG MGVDKPDIRY
VIHFHLPQTA EAFMQEIGRA GRDGKPSVSI LLRAPGDFEL QEQIIQMESV TAEEIADVIR
VLEKTEERDE RRLRDVLLQY GVGETQARMM IHLFMQGKTS VELMKKEISY RMELKLEKMH
RVSFLLQRDG CLRQALLTYF DESYEPDDGN LPCCSHCGFD LSLYEQKGER SKMAPLDSWS
SELHRIFSLQ TVGELN
