MFD_STAA3
ID MFD_STAA3 Reviewed; 1168 AA.
AC Q2FJD8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
GN OrderedLocusNames=SAUSA300_0481;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD21284.1; -; Genomic_DNA.
DR RefSeq; WP_000154228.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FJD8; -.
DR SMR; Q2FJD8; -.
DR PRIDE; Q2FJD8; -.
DR EnsemblBacteria; ABD21284; ABD21284; SAUSA300_0481.
DR KEGG; saa:SAUSA300_0481; -.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OMA; WAPPCRE; -.
DR Proteomes; UP000001939; 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..1168
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000282675"
FT DOMAIN 633..794
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 808..969
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 747..750
FT /note="DEEQ box"
FT BINDING 646..653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1168 AA; 134219 MW; AEA8E7999E478C4E CRC64;
MTILTTLIKE DNHFQDLNQV FGQANTLVTG LSPSAKVTMI AEKYAQSNQQ LLLITNNLYQ
ADKLETDLLQ FIDAEELYKY PVQDIMTEEF STQSPQLMSE RIRTLTALAQ GKKGLFIVPL
NGLKKWLTPV EMWQNHQMTL RVGEDIDVDQ FLNKLVNMGY KRESVVSHIG EFSLRGGIID
IFPLIGEPIR IELFDTEIDS IRDFDVETQR SKDNVEEVDI TTASDYIITE EVISHLKEEL
KTAYENTRPK IDKSVRNDLK ETYESFKLFE STYFDHQILR RLVAFMYETP STIIEYFQKD
AIIAVDEFNR IKETEESLTV ESDSFISNII ESGNGFIGQS FIKYDDFETL IEGYPVTYFS
LFATTMPIKL NHIIKFSCKP VQQFYGQYDI MRSEFQRYVN QNYHIVVLVE TETKVERMQA
MLSEMHIPSI TKLHRSMSSG QAVIIEGSLS EGFELPDMGL VVITERELFK SKQKKQRKRT
KAISNAEKIK SYQDLNVGDY IVHVHHGVGR YLGVETLEVG QTHRDYIKLQ YKGTDQLFVP
VDQMDQVQKY VASEDKTPKL NKLGGSEWKK TKAKVQQSVE DIAEELIDLY KEREMAEGYQ
YGEDTAEQTT FELDFPYELT PDQAKSIDEI KDDMQKSRPM DRLLCGDVGY GKTEVAVRAA
FKAVMEGKQV AFLVPTTILA QQHYETLIER MQDFPVEIQL MSRFRTPKEI KQTKEGLKTG
FVDIVVGTHK LLSKDIQYKD LGLLIVDEEQ RFGVRHKERI KTLKHNVDVL TLTATPIPRT
LHMSMLGVRD LSVIETPPEN RFPVQTYVLE QNMSFIKEAL ERELSRDGQV FYLYNKVQSI
YEKREQLQML MPDANIAVAH GQMTERDLEE TMLSFINNEY DILVTTTIIE TGVDVPNANT
LIIEDADRFG LSQLYQLRGR VGRSSRIGYA YFLHPANKVL TETAEDRLQA IKEFTELGSG
FKIAMRDLNI RGAGNLLGKQ QHGFIDTVGF DLYSQMLEEA VNEKRGIKEP ESEVPEVEVD
LNLDAYLPTE YIANEQAKIE IYKKLRKTET FDQIIDIKDE LIDRFNDYPV EVARLLDIVE
IKVHALHSGI TLIKDKGKII DIHLSVKATE NIDGEVLFKA TQPLGRTMKV GVQNNAMTIT
LTKQNQWLDS LKFLVKCIEE SMRISDEA
