ID   MFD_BACSU               Reviewed;        1177 AA.
AC   P37474;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; OrderedLocusNames=BSU00550;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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).
CC   -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC       polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC       release of RNAP and its truncated transcript from the DNA, and
CC       recruitment of nucleotide excision repair machinery to the damaged
CC       site. {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}.
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DR   EMBL; D26185; BAA05290.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11831.1; -; Genomic_DNA.
DR   PIR; S66085; S66085.
DR   RefSeq; NP_387936.1; NC_000964.3.
DR   RefSeq; WP_003243453.1; NZ_JNCM01000028.1.
DR   AlphaFoldDB; P37474; -.
DR   SMR; P37474; -.
DR   STRING; 224308.BSU00550; -.
DR   PaxDb; P37474; -.
DR   PRIDE; P37474; -.
DR   DNASU; 936653; -.
DR   EnsemblBacteria; CAB11831; CAB11831; BSU_00550.
DR   GeneID; 936653; -.
DR   KEGG; bsu:BSU00550; -.
DR   PATRIC; fig|224308.179.peg.55; -.
DR   eggNOG; COG1197; Bacteria.
DR   InParanoid; P37474; -.
DR   OMA; WAPPCRE; -.
DR   PhylomeDB; P37474; -.
DR   BioCyc; BSUB:BSU00550-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043175; F:RNA polymerase core enzyme binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   Gene3D; 3.90.1150.50; -; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR004576; Mfd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00982; TRCF; 1.
DR   SUPFAM; SSF141259; SSF141259; 1.
DR   SUPFAM; SSF143517; SSF143517; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00580; mfd; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1177
FT                   /note="Transcription-repair-coupling factor"
FT                   /id="PRO_0000102162"
FT   DOMAIN          638..799
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   DOMAIN          820..974
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   MOTIF           752..755
FT                   /note="DEEQ box"
FT   BINDING         651..658
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ   SEQUENCE   1177 AA;  133812 MW;  70938BC354424687 CRC64;
     MDNIQTFIKE SDDFKSIING LHEGLKEQLL AGLSGSARSV FTSALANETN KPIFLITHNL
     YQAQKVTDDL TSLLEDRSVL LYPVNELISS EIAVASPELR AQRLDVINRL TNGEAPIVVA
     PVAAIRRMLP PVEVWKSSQM LIQVGHDIEP DQLASRLVEV GYERSDMVSA PGEFSIRGGI
     IDIYPLTSEN PVRIELFDTE VDSIRSFNSD DQRSIETLTS INIGPAKELI IRPEEKARAM
     EKIDSGLAAS LKKLKADKQK EILHANISHD KERLSEGQTD QELVKYLSYF YEKPASLLDY
     TPDNTLLILD EVSRIHEMEE QLQKEEAEFI TNLLEEGKIL HDIRLSFSFQ KIVAEQKRPL
     LYYSLFLRHV HHTSPQNIVN VSGRQMQSFH GQMNVLAGEM ERFKKSNFTV VFLGANKERT
     QKLSSVLADY DIEAAMTDSK KALVQGQVYI MEGELQSGFE LPLMKLAVIT EEELFKNRVK
     KKPRKQKLTN AERIKSYSEL QIGDYVVHIN HGIGKYLGIE TLEINGIHKD YLNIHYQGSD
     KLYVPVEQID QVQKYVGSEG KEPKLYKLGG SEWKRVKKKV ETSVQDIADD LIKLYAEREA
     SKGYAFSPDH EMQREFESAF PYQETEDQLR SIHEIKKDME RERPMDRLLC GDVGYGKTEV
     AIRAAFKAIG DGKQVALLVP TTILAQQHYE TIKERFQDYP INIGLLSRFR TRKEANETIK
     GLKNGTVDIV IGTHRLLSKD VVYKDLGLLI IDEEQRFGVT HKEKIKQIKA NVDVLTLTAT
     PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEYNGAL VREAIERELA RGGQVYFLYN
     RVEDIERKAD EISMLVPDAK VAYAHGKMTE NELETVMLSF LEGESDVLVS TTIIETGVDI
     PNVNTLIVFD ADKMGLSQLY QLRGRVGRSN RVAYAYFTYR RDKVLTEVAE KRLQAIKEFT
     ELGSGFKIAM RDLTIRGAGN LLGAQQHGFI DSVGFDLYSQ MLKEAIEERK GDTAKTEQFE
     TEIDVELDAY IPETYIQDGK QKIDMYKRFR SVATIEEKNE LQDEMIDRFG NYPKEVEYLF
     TVAEMKVYAR QERVELIKQD KDAVRLTISE EASAEIDGQK LFELGNQYGR QIGLGMEGKK
     LKISIQTKGR SADEWLDTVL GMLKGLKDVK KQTISST