MFD_BORBU
ID MFD_BORBU Reviewed; 1125 AA.
AC O51568;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=BB_0623;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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; AE000783; AAC66973.1; -; Genomic_DNA.
DR PIR; F70177; F70177.
DR RefSeq; NP_212757.1; NC_001318.1.
DR RefSeq; WP_010889782.1; NC_001318.1.
DR AlphaFoldDB; O51568; -.
DR SMR; O51568; -.
DR STRING; 224326.BB_0623; -.
DR PRIDE; O51568; -.
DR EnsemblBacteria; AAC66973; AAC66973; BB_0623.
DR KEGG; bbu:BB_0623; -.
DR PATRIC; fig|224326.49.peg.1013; -.
DR HOGENOM; CLU_005122_1_3_12; -.
DR OMA; SHVVHIN; -.
DR Proteomes; UP000001807; 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 transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
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..1125
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000102163"
FT DOMAIN 597..758
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 774..933
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 711..714
FT /note="DEEQ box"
FT BINDING 610..617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1125 AA; 130730 MW; 116FBF8DE9024539 CRC64;
MNIDEELTTI LKNNSNLKKM KEFLEQNIFF SLTGYEGFFK AFLIKKIKEY SKTGKIILIV
KDEHTLDKIK NDLQVITNQI FELNYFSPLV YKGIGSKSTI FNERIKFLFN FYKKNPGIYI
TVLKSLLSKI PDKNTLLKNI YKIEKNTNIN TADIEKTLIT LGYEKTLRVT IPGEFTVKGE
IIDIYPFGEQ NPIRIALNFD KIEEIKKFNP LTQLKHDNEI LEFQILPKKE IIWDDKTINT
LKTKIKSVEY KKILEELDFK KETKTEEMFY PLVANTYLGD EIEKHTPIVN FEINNFEKEI
EKIHQEYEKL YKEAEEAGKN IIDPKRILLN YKTFNLKSDV LFSKIKSLKS KETIEFKIES
ERNFFSNIAL TKEEFENWLK NGFKIIIAAE SESQKEKLKY IFKELPKVSI EVLKISSSLI
IEKEKIAIIL ESNIFNTGQK INKAFESSKT KAIDSFVEIE KNSHVVHINH GIGIFRQIKR
IKTSSLEKDY IEIEYAEGEK LFIPIEQTNL IQKYIGSDPK NIKLDKISSK TWIKNKANAK
KRIEEIADKL IELYSKRESI KGIKYPEDNE LQLLFESEFP YDETPDQIRA IKEIKEDMMS
FKVMDRLLCG DVGFGKTEVA MRAAFKAVMG NKQVIVLSPT TILAEQHFNT FKKRFKNFPI
KIEVLSRFIK NNAESRILKE LKSGKIDIII GTHKILSKKF TCKNLGLIII DEEQRFGVKE
KEKLKEIRIS VDCLALSATP IPRSLHMSLI KLRDISVLKI PPQNRVKIEA YLESFSELLI
KHAIESELSR DGQVFLVNHN IEELYYLKTL IERLTPYARI AIIHGKLTGE EIENIMHNFI
KKAYQILLAT TIIENGIDIP NANTIIINNA NKFGLAQLYQ LKGRVGRGSQ KAYAYFLYQD
SEKLNERSIE RLRAITEFSE LGAGFKIAMK DMEIRGVGNL LGREQHGEIE SIGLDYYLTM
LNKAIEKKMG KISSDEEEVD IKINYSGFIP ENYAKNEQDK ILIYKKIFKI QTEEESKKIR
SELHNDFGPI PEEINSLLML AELKILAKDL NITKLKEKNR ALEIEYKNIE SIPMEKIIEI
LQKHPNLLIL NPSYQKSIFL SFKNIEKSEK INYIYKNINL LKTST
