MFD_STAHJ
ID MFD_STAHJ Reviewed; 1169 AA.
AC Q4L3G0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=SH2508;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05817.1; -; Genomic_DNA.
DR RefSeq; WP_011276758.1; NC_007168.1.
DR AlphaFoldDB; Q4L3G0; -.
DR SMR; Q4L3G0; -.
DR STRING; 279808.SH2508; -.
DR PRIDE; Q4L3G0; -.
DR EnsemblBacteria; BAE05817; BAE05817; SH2508.
DR KEGG; sha:SH2508; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OMA; WAPPCRE; -.
DR OrthoDB; 234717at2; -.
DR Proteomes; UP000000543; 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.
FT CHAIN 1..1169
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000282678"
FT DOMAIN 634..795
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 809..970
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 748..751
FT /note="DEEQ box"
FT BINDING 647..654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1169 AA; 134926 MW; 26462584C1D22465 CRC64;
MRPIISDYIQ NDKRFQELDD VFGHQNILVT GLSPSAKATI IAEKYLKDQK QMLLITNNLY
QADKLETDIL QYIDHSEVYK YPVQDIMTEE FSTQSPQLMS ERVRTLTALA HNKKGLFIVP
LNGLKKWLTP FELWKDHQIT LRVGEDIDVD EFLNKLVNMG YRRESVVSHI GEFSLRGGII
DIYPLIGQPV RIELFDTEVD SIRDFDVETQ RSNDNIEEVS ITTASDYVIT DDVIQHLQSE
LKTAYEATRP KIDKSVRNDL KETYESFKLF ETTFFDHQLL RRLVAFMYEQ PSTLIDYFAK
DAIIVADEYN RIKETEKTLT TEVDDFIQNL IESGNGFIGQ SFMQYDGFES LLKDYPVTYF
TLFTSTMPVQ LQHIIKFSCK PVQQFYGQYD IMRSEFQRYV HNDYHIVVLV ETETKVERIQ
SMLNEMHIPT VTNVQNDIKS GQVVVTEGSL SEGFELPYMQ LVVITERELF KTKQKKQRKR
TKTLSNAEKI KSYQDLNVGD YVVHVHHGVG RYLGVETLEV GDVHRDYIKL QYKGTDQLFV
PVDQMDQVQK YVASEDKSPK LNKLGGSEWK KTKAKVQQSV EDIADELIAL YKEREMSVGY
QYGEDTAEQS AFEMDFPYEL TPDQAKSIDE IKGDMERERP MDRLLCGDVG YGKTEVAVRA
AFKAVMEGKQ VAFLVPTTIL AQQHYETLIE RMQDFPVQIE LISRFRSTKE VKETKEGLKS
GYVDIVVGTH KLLGKDIHYK DLGLLIVDEE QRFGVRHKER IKTMKTNVDV LTLTATPIPR
TLHMSMLGVR DLSVIETPPE NRFPVQTYVL EQNSNFIKEA LERELSRDGQ VFYLYNRVQS
IYEKREQLQM LMPDANIAVA HGQMTERDLE ETMLSFINGE FDILVTTTII ETGVDVPNAN
TLIIEEADRF GLSQLYQLRG RVGRSSRIGY AYFLHSANKV LTETAEERLQ AIKEFTELGS
GFKIAMRDLN IRGAGNLLGK QQHGFIDSVG FDLYSQMLEE AVNEKRGIKE EEPDAPEVEM
ELNLDAYLPA EYIQNEQAKI EIYKKLRKVE TEEQLFDIKD ELIDRFNDYP VEVERLLEMV
EIKIHALHAG VTLIKDKGKQ IEVSLSTKAT EQMNGEELFK QTQPLGRAMK LGVKENRMHV
TLTKSKQWLD NLKFLVRCLE GSMVIEDEN
