MFD_STAES
ID MFD_STAES Reviewed; 1169 AA.
AC Q8CMT1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=SE_2280;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05922.1; -; Genomic_DNA.
DR RefSeq; NP_765835.1; NC_004461.1.
DR RefSeq; WP_011082820.1; NZ_WBME01000023.1.
DR AlphaFoldDB; Q8CMT1; -.
DR SMR; Q8CMT1; -.
DR STRING; 176280.SE_2280; -.
DR EnsemblBacteria; AAO05922; AAO05922; SE_2280.
DR KEGG; sep:SE_2280; -.
DR PATRIC; fig|176280.10.peg.2223; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OMA; WAPPCRE; -.
DR Proteomes; UP000001411; 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_0000282676"
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; 134745 MW; 551B1F6670DBB591 CRC64;
MKSMIANYIS EDNRFQELDE VFGQENILVT GLSPSAKATI IAEKYLKDHK QMLLVTNNLY
QADKIETDIL QYVDDSEVYK YPVQDIMTEE FSTQSPQLMS ERVRTLTALA QGEKGLFIVP
LNGFKKWLTP VDLWKDHQMT LKVGQDIDVD AFLNKLVNMG YRRESVVSHI GEFSLRGGII
DIYPLIGTPV RIELFDTEVD SIRDFDVETQ RSNDNINQVE ITTASDYIIT DEVIQHLQNE
LKKAYEYTRP KIEKSVRNDL KETYESFKLF ESTFFDHQLL RRLVSFMYEK PSTLIDYFQK
NAIIVVDEFN RIKETEETLT TEVEDFMSNL IESGNGFIGQ GFMKYESFDA LLEQHAVAYF
TLFTSSMQVP LQHIIKFSCK PVQQFYGQYD IMRSEFQRYV HQDYTVVVLV ETETKVERIQ
SMLNEMHIPT VSNIHEDIDG GQVVVTEGSL SEGFELPYMQ LVVITERELF KTRQKKQRKR
TKTISNAEKI KSYQDLNVGD YIVHVHHGVG RYLGVETLEV GDTHRDYIKL QYKGTDQLFV
PVDQMDQVQK YVASEDKSPR LNKLGGTEWK KTKAKVQQSV EDIADELIDL YKEREMSVGY
QYGQDTAEQS AFEHDFPYEL TPDQSKSIDE IKGDMERARP MDRLLCGDVG YGKTEVAVRA
AFKAVMDGKQ VAFLVPTTIL AQQHYETLLE RMQDFPVEIQ LVSRFRTAKE IRETKEGLKS
GYVDIVVGTH KLLGKDIQYK DLGLLIVDEE QRFGVRHKER IKTLKKNVDV LTLTATPIPR
TLHMSMLGVR DLSVIETPPE NRFPVQTYVL EQNTNFIKEA LERELSRDGQ VFYLYNKVQS
IYEKREQLQR LMPDANIAVA HGQMTERDLE ETMLSFINHE YDILVTTTII ETGVDVPNAN
TLIIEEADRF GLSQLYQLRG RVGRSSRIGY AYFLHPANKV LNETAEERLQ TIKEFTELGS
GFKIAMRDLN IRGAGNLLGK QQHGFIDSVG FDLYSQMLEE AVNEKRGIKE ESPDAPDIEV
ELHLDAYLPA EYIQSEQAKI EIYKKLRKVE TEEQLFDVKD ELIDRFNDYP IEVERLLDIV
EIKVHALHAG VELIKDKGKS IQIILSPKAT EDINGEELFK QTQPLGRAMK VGVQNNAMNV
TLTKSKQWLD SLKFLVRCIE ESMAIKDED
