MFD_MYCTU
ID MFD_MYCTU Reviewed; 1234 AA.
AC P9WMQ5; L0T5H3; P64326; P96380;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv1020;
GN ORFNames=MTCY10G2.29c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP INTERACTION WITH RPOB.
RC STRAIN=Erdman;
RX PubMed=22904282; DOI=10.1128/jb.00879-12;
RA Weiss L.A., Harrison P.G., Nickels B.E., Glickman M.S., Campbell E.A.,
RA Darst S.A., Stallings C.L.;
RT "Interaction of CarD with RNA polymerase mediates Mycobacterium
RT tuberculosis viability, rifampicin resistance, and pathogenesis.";
RL J. Bacteriol. 194:5621-5631(2012).
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 -!- SUBUNIT: Interacts with the RNA polymerase subunit beta (RpoB).
CC {ECO:0000269|PubMed:22904282}.
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; AL123456; CCP43770.1; -; Genomic_DNA.
DR PIR; G70622; G70622.
DR RefSeq; NP_215536.1; NC_000962.3.
DR RefSeq; WP_003405273.1; NZ_NVQJ01000018.1.
DR PDB; 6ACA; X-ray; 3.60 A; A=1-1234.
DR PDBsum; 6ACA; -.
DR AlphaFoldDB; P9WMQ5; -.
DR SMR; P9WMQ5; -.
DR IntAct; P9WMQ5; 1.
DR STRING; 83332.Rv1020; -.
DR PaxDb; P9WMQ5; -.
DR DNASU; 886077; -.
DR GeneID; 886077; -.
DR KEGG; mtu:Rv1020; -.
DR TubercuList; Rv1020; -.
DR eggNOG; COG1197; Bacteria.
DR OMA; WAPPCRE; -.
DR PhylomeDB; P9WMQ5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1234
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000102170"
FT DOMAIN 663..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 842..999
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT REGION 1207..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 777..780
FT /note="DEEQ box"
FT BINDING 676..683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1234 AA; 132908 MW; DBE48CE5ACF42B7D CRC64;
MTAPGPACSD TPIAGLVELA LSAPTFQQLM QRAGGRPDEL TLIAPASARL LVASALARQG
PLLVVTATGR EADDLAAELR GVFGDAVALL PSWETLPHER LSPGVDTVGT RLMALRRLAH
PDDAQLGPPL GVVVTSVRSL LQPMTPQLGM MEPLTLTVGD ESPFDGVVAR LVELAYTRVD
MVGRRGEFAV RGGILDIFAP TAEHPVRVEF WGDEITEMRM FSVADQRSIP EIDIHTLVAF
ACRELLLSED VRARAAQLAA RHPAAESTVT GSASDMLAKL AEGIAVDGME AVLPVLWSDG
HALLTDQLPD GTPVLVCDPE KVRTRAADLI RTGREFLEAS WSVAALGTAE NQAPVDVEQL
GGSGFVELDQ VRAAAARTGH PWWTLSQLSD ESAIELDVRA APSARGHQRD IDEIFAMLRA
HIATGGYAAL VAPGTGTAHR VVERLSESDT PAGMLDPGQA PKPGVVGVLQ GPLRDGVIIP
GANLVVITET DLTGSRVSAA EGKRLAAKRR NIVDPLALTA GDLVVHDQHG IGRFVEMVER
TVGGARREYL VLEYASAKRG GGAKNTDKLY VPMDSLDQLS RYVGGQAPAL SRLGGSDWAN
TKTKARRAVR EIAGELVSLY AKRQASPGHA FSPDTPWQAE LEDAFGFTET VDQLTAIEEV
KADMEKPIPM DRVICGDVGY GKTEIAVRAA FKAVQDGKQV AVLVPTTLLA DQHLQTFGER
MSGFPVTIKG LSRFTDAAES RAVIDGLADG SVDIVIGTHR LLQTGVRWKD LGLVVVDEEQ
RFGVEHKEHI KSLRTHVDVL TMSATPIPRT LEMSLAGIRE MSTILTPPEE RYPVLTYVGP
HDDKQIAAAL RRELLRDGQA FYVHNRVSSI DAAAARVREL VPEARVVVAH GQMPEDLLET
TVQRFWNREH DILVCTTIVE TGLDISNANT LIVERADTFG LSQLHQLRGR VGRSRERGYA
YFLYPPQVPL TETAYDRLAT IAQNNELGAG MAVALKDLEI RGAGNVLGIE QSGHVAGVGF
DLYVRLVGEA LETYRDAYRA AADGQTVRTA EEPKDVRIDL PVDAHLPPDY IASDRLRLEG
YRRLAAASSD REVAAVVDEL TDRYGALPEP ARRLAAVARL RLLCRGSGIT DVTAASAATV
RLSPLTLPDS AQVRLKRMYP GAHYRATTAT VQVPIPRAGG LGAPRIRDVE LVQMVADLIT
ALAGKPRQHI GITNPSPPGE DGRGRNTTIK ERQP
