ID A0A0H3E8Q8_BACA1 Unreviewed; 1177 AA.
AC A0A0H3E8Q8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN OrderedLocusNames=BATR1942_18885 {ECO:0000313|EMBL:ADP34694.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP34694.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP34694.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP34694.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR EMBL; CP002207; ADP34694.1; -; Genomic_DNA.
DR RefSeq; WP_003328577.1; NC_014639.1.
DR AlphaFoldDB; A0A0H3E8Q8; -.
DR GeneID; 23412188; -.
DR KEGG; bae:BATR1942_18885; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006867; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR CDD; cd18810; SF2_C_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11140; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
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; IPR048635; MFD_D3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21132; MFD_D3; 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; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 820..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1177 AA; 133847 MW; 9572FB6E4E4E4087 CRC64;
MDNIQTFIKE SDDFKSIVTG LHEGLREQLL AGLSGSARSV FTSALSEKIN QPIFLITHNL
YQAQKVTEDL TALLEDQSVL LYPVNELISS EIAVASPELR AQRLDVINRL TAGETPIVVA
PVAAVRRMLP PVDVWKNSQM TITTGEDIEP DQLSSRLVEV GYERSDMVSA PGEFSIRGGI
IDIYPLTAEH PVRIELFDTE VDSIRTFNSD DQRSIETLTS VSIGPAKELI IRAEEKARAI
EKIDKGLAAS LKKVKADKQK EILHMNISHD KERLSEGQTD QELVKYLSYF YEKPASLLDY
TPPDTLLLLD EVSRIHEMEE QLQKEEAEFV TNLLEEGKIL HDISLSFSFQ NLVSKQQRPI
LYYSLFLRHV QHTSPQNIVN VSSRQMQSFH GQMNVLASEM ERFKKSNFTV IFLGANKERT
ERLSSVLADY EIEAAMIDNK KALAQGQVYV MEGELQSGFE LPLMKLAVIT EEELFKNRMK
KKPRKQKITN AERIKSYSEL QVGDYVVHVN HGIGKYLGIE TLEINGIHKD YLNIHYQGSD
KLYVPVEQID QVQKYVGSEG KEPKLYKLGG SEWKRVKKKV ETSVQDIADD LIKLYAEREA
SKGYAFSPDH EMQREFESAF PYQETEDQLR SINEIKKDME RERPMDRLLC GDVGYGKTEV
AIRAAFKAIA DGKQVALLVP TTILAQQHYE TIMERFQDYP LTVGLLSRFR TRKEANETIK
GLKNGTVDMV IGTHRLLSKD VVYKDLGLLI IDEEQRFGVT HKEKIKQIKA NVDVLTLTAT
PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEYNGAL VREAIERELA RGGQVYFLYN
RVDDIERKAD EISMLVPDAK VAYAHGKMTE NELESVMLNF LEGESDVLVS TTIIETGVDI
PNVNTLIVFD GDKMGLSQLY QLRGRVGRSN RVAYAYFTYR RDKVLTEVAE KRLQAIKEFT
ELGSGFKIAM RDLTIRGAGN LLGAQQHGFI DSVGFDLYSQ MLKEAIEERR GDTSKSEQFE
TEIDVELDAY IPETYIQDGK QKIDMYKRFR SVATLEEKNE LQDEMIDRFG NYPKEVEYLF
TVAEMKVYAK NERVELIKQD KDAVRFTITE SASAEIDGQK LFELGNKYGR QIGLGMEGKK
LKISIQTKGR KTDEWLETVL GMLKGLKKVK KQTIASS
//
