ID   RECQ_BACSU              Reviewed;         591 AA.
AC   O34748; Q796C5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable ATP-dependent DNA helicase RecQ;
DE            EC=3.6.4.12;
GN   Name=recQ; Synonyms=yocI; OrderedLocusNames=BSU19220;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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   IDENTIFICATION.
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, SUBCELLULAR LOCATION, 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 for DNA repair and
CC       intramolecular recombination; probably has overlapping function with
CC       RecS (AC P50729). It probably acts to help generate ss-DNA from ds-DNA
CC       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   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC       {ECO:0000269|PubMed:16385024}. Note=Localized throughout the nucleoid
CC       in the presence or absence of DNA double-strand breaks.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are moderately sensitive
CC       to DNA-damaging agents. Sensitivity increases in the presence of
CC       mutated AddAB nuclease. {ECO:0000269|PubMed:16385024}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ 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; AF027868; AAB84475.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13814.1; -; Genomic_DNA.
DR   PIR; F69901; F69901.
DR   RefSeq; NP_389803.1; NC_000964.3.
DR   RefSeq; WP_004399229.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34748; -.
DR   SMR; O34748; -.
DR   STRING; 224308.BSU19220; -.
DR   PaxDb; O34748; -.
DR   PRIDE; O34748; -.
DR   EnsemblBacteria; CAB13814; CAB13814; BSU_19220.
DR   GeneID; 939671; -.
DR   KEGG; bsu:BSU19220; -.
DR   PATRIC; fig|224308.179.peg.2100; -.
DR   eggNOG; COG0514; Bacteria.
DR   InParanoid; O34748; -.
DR   OMA; HHDIPKS; -.
DR   PhylomeDB; O34748; -.
DR   BioCyc; BSUB:BSU19220-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; IDA:UniProtKB.
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   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.80; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47819; SSF47819; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01389; recQ; 1.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN           1..591
FT                   /note="Probable ATP-dependent DNA helicase RecQ"
FT                   /id="PRO_0000379511"
FT   DOMAIN          27..196
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          216..367
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          513..591
FT                   /note="HRDC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT   MOTIF           139..142
FT                   /note="DEAH box"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   591 AA;  67353 MW;  D66395DD59153626 CRC64;
     MLHRAQSLLA HYFGYEKFRS GQDEAIRLVT EARQNTACIM PTGGGKSICY QIPALMFEGT
     TIVISPLISL MKDQVDALEE AGINAAYINS TQSNQEIYER LNGLKEGAYK LFYITPERLT
     SIEFIRILQG IDVPLVAIDE AHCISQWGHD FRPSYRNIEI LFRELHDKPV IMALTATATP
     EVHDDICKQL HIQKENTVYT GFSRENLTFK VVKGENKDRF IDEYVQNNRH EAGIVYTATR
     KEADRIYERL KRNQVRAGRY HGGLADDVRK EQQERFLNDE LQVMVATSAF GMGIDKSNIR
     FVLHAQIPKD MESYYQEAGR AGRDGLASEC VLLFSPQDIM VQRFLIEQSE HEEKQKQDLK
     KLRQMVDYCH TEDCLQRFIL MYFGEKEPDA CGQCGNCTDT RAAHDVTREA QMVLSCIIRM
     KERFGKTMVA QVLAGSKNKK VLENGFSDLS TYGILKHQSV GEISDFIEFL ISDDFIRMSD
     GTFPTLFVSS KGRNVLKGEL SVARKEALKA AAITENDELF ERLRMVRKEI AAEQGVPPFV
     VFSDQTLKEM SGKQPVNDDE LLSIKGVGEQ KRAKYGRLFL QEIQAYARMT D