ID Q8DRQ1_STRR6 Unreviewed; 1169 AA.
AC Q8DRQ1;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 155.
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 ECO:0000313|EMBL:AAK98810.1};
GN OrderedLocusNames=spr0006 {ECO:0000313|EMBL:AAK98810.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK98810.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK98810.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2] {ECO:0007829|PDB:2QSR}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1007-1168.
RA Ramagopal U.A., Toro R., Gilmore M., Bain K., Iizuka M., Wasserman S.,
RA Rodgers L., Sauder J.M., Burley S.K., Almo S.C.;
RT "Structure of C-terminal domain of transcription-repair coupling factor.";
RL Submitted (JUL-2007) to the PDB data bank.
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}.
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; AE007317; AAK98810.1; -; Genomic_DNA.
DR PIR; F97872; F97872.
DR RefSeq; NP_357600.1; NC_003098.1.
DR RefSeq; WP_000258109.1; NC_003098.1.
DR PDB; 2QSR; X-ray; 3.10 A; A=1007-1168.
DR PDBsum; 2QSR; -.
DR AlphaFoldDB; Q8DRQ1; -.
DR SMR; Q8DRQ1; -.
DR STRING; 171101.spr0006; -.
DR DNASU; 933199; -.
DR KEGG; spr:spr0006; -.
DR PATRIC; fig|171101.6.peg.6; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_1_9; -.
DR EvolutionaryTrace; Q8DRQ1; -.
DR Proteomes; UP000000586; 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 DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 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; 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; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2QSR};
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}; Reference proteome {ECO:0000313|Proteomes:UP000000586}.
FT DOMAIN 627..788
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 809..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1169 AA; 134802 MW; F6FB4B08C55F8495 CRC64;
MVTLLDLFSE NDQIKKWHQN LTDKKRQLIL GLSTSTKALA IASSLEKEDR IVLLTSTYGE
AEGLVSDLIS ILGEELVYPF LVDDAPMVEF LMSSQEKIIS RVEALRFLTD SSKKGILVCN
IAASRLILPS PNAFKDSIVK ISVGEEYDQH AFIHQLKENG YRKVTQVQTQ GEFSLRGDIL
DIFEISQLEP CRIEFFGDEI DGIRSFEVET QLSKENKTEL TIFPASDMLL REKDYQRGQS
ALEKQISKTL SPILKSYLEE ILSSFHQKQS HADSRKFLSL CYDKTWTVFD YIEKDTPIFF
DDYQKLMNQY EVFERELAQY FTEELQNSKA FSDMQYFSDI EQIYKKQSPV TFFSNLQKGL
GNLKFDKIYQ FNQYPMQEFF NQFSFLKEEI ERYKKMDYTI ILQSSNSMGS KTLEDMLEEY
QIKLDSRDKT SICKESVNLI EGNLRHGFHF VDEKILLITE HEIFQKKLKR RFRRQHVSNA
ERLKDYNELE KGDYVVHHIH GIGQYLGIET IEIKEIHRDY VSVQYQNGDQ ISIPVEQIHL
LSKYISSDGK APKLNKLNDG HFKKAKQKVK NQVEDIADDL IKLYSERSQL KGFAFSADDD
DQDAFDDAFP YVETDDQLRS IEEIKRDMQA SQPMDRLLVG DVGFGKTEVA MRAAFKAVND
HKQVVILVPT TVLAQQHYTN FKERFQNFAV NVDVLSRFRS KKEQTATLEK LKNGQVDILI
GTHRVLSKDV VFADLGLMII DEEQRFGVKH KETLKELKKQ VDVLTLTATP IPRTLHMSML
GIRDLSVIET PPTNRYPVQT YVLEKNDSVI RDAVLREMER GGQGYYLYNK VDTIVQKVSE
LQELIPEASI GYVHGRMSEV QLENTLLDFI EGQYDILVTT TIIETGVDIP NANTLFIENA
DHMGLSTLYQ LRGRVGRSNR IAYAYLMYRP EKSISEVSEK RLEAIKGFTE LGSGFKIAMR
DLSIRGAGNL LGKSQSGFID SVGFELYSQL LEEAIAKRNG NANANTRTKG NAELILQIDA
YLPDTYISDQ RHKIEIYKKI RQIDNRVNYE ELQEELIDRF GEYPDVVAYL LEIGLVKSYL
DKVFVQRVER KDNKITIQFE KVTQRLFLAQ DYFKALSVTN LKAGIAENKG LMELVFDVQN
KKDYEILEGL LIFGESLLEI KESKEKNSI
//
