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 01-MAY-2013, entry version 95.
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
RT the 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.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA 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.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA 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;
RA Fernandez S., Sorokin A., Alonso J.C.;
RT "Genetic recombination in Bacillus subtilis 168: effects of recU and
RT recS 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
RT the 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
CC with RecS (AC P50729). It probably acts to help generate ss-DNA
CC from ds-DNA breaks.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Note=Localized
CC throughout the nucleoid in the presence or absence of DNA double-
CC strand breaks.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are moderately
CC sensitive to DNA-damaging agents. Sensitivity increases in the
CC presence of mutated AddAB nuclease.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 HRDC domain.
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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 HSSP; P15043; 1WUD.
DR ProteinModelPortal; O34748; -.
DR SMR; O34748; 1-506, 515-590.
DR STRING; 224308.BSU19220; -.
DR PaxDb; O34748; -.
DR EnsemblBacteria; CAB13814; CAB13814; BSU19220.
DR GeneID; 939671; -.
DR KEGG; bsu:BSU19220; -.
DR PATRIC; 18975693; VBIBacSub10457_2037.
DR GenoList; BSU19220; -.
DR eggNOG; COG0514; -.
DR HOGENOM; HOG000044388; -.
DR KO; K03654; -.
DR OMA; HAAYINS; -.
DR ProtClustDB; CLSK887416; -.
DR BioCyc; BSUB:BSU19220-MONOMER; -.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 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; SSF47819; HRDC_like; 1.
DR TIGRFAMs; TIGR01389; recQ; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
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; Complete proteome; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1 591 Probable ATP-dependent DNA helicase RecQ.
FT /FTId=PRO_0000379511.
FT DOMAIN 27 196 Helicase ATP-binding.
FT DOMAIN 216 367 Helicase C-terminal.
FT DOMAIN 513 591 HRDC.
FT NP_BIND 40 47 ATP (By similarity).
FT MOTIF 139 142 DEAH box.
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
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