ID   MFD_BUCBP               Reviewed;         697 AA.
AC   Q89AK2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Transcription-repair-coupling factor;
DE            Short=TRCF;
DE            EC=3.6.4.-;
GN   Name=mfd; OrderedLocusNames=bbp_275;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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 site
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27000.1; -; Genomic_DNA.
DR   RefSeq; WP_011091401.1; NC_004545.1.
DR   AlphaFoldDB; Q89AK2; -.
DR   SMR; Q89AK2; -.
DR   STRING; 224915.bbp_275; -.
DR   EnsemblBacteria; AAO27000; AAO27000; bbp_275.
DR   GeneID; 56470816; -.
DR   KEGG; bab:bbp_275; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_8_2_6; -.
DR   OMA; CYAVIPA; -.
DR   OrthoDB; 234717at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   Gene3D; 3.90.1150.50; -; 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   Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 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; 2.
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; Reference proteome.
FT   CHAIN           1..697
FT                   /note="Transcription-repair-coupling factor"
FT                   /id="PRO_0000102165"
FT   DOMAIN          168..329
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          350..504
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           282..285
FT                   /note="DEEH box"
FT   BINDING         181..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   697 AA;  80419 MW;  DF4C7E23C4FADBE7 CRC64;
     MLIKSLVQKN QVYFTNNSLD EKNICDLSKL KINQPIVHFE HGVGRYQGLT TVTTRNIKTE
     CVVINYAQNS KLYVPITYLY LISRYIGTSK KDIPLHRLGN DLWNKEKKKA NEKAYDSAAI
     LLNIYSHRIS QKGFSFKKHH TKYKIFCERF PFTLTPDQDS AINSVLSDMY KSTPMDRLVC
     GDVGFGKTEV AMRATFLAVC NQKQVAILVP TTLLAQQHFN NFTLRFKYWS TKIEILSRFQ
     SETKCNEIIN NVNIGNVHVL IGTHKILLKN LKWKNLGLLI VDEEHRFGVH HKEQIKLISN
     NIDVLTLTAT PIPRTLNMAF VGIRDLSIIA TPPKQRLIVK TFVREFSYTV IRKAILREIL
     RGGQVYYIYN NVNKIERKKI ELKKLVPEAN IRIGHGQLRS TDLESIMNDF YHKRFNVLVC
     STIIETGIDI PNVNTIIIEN ANNFGLAQLH QLRGRVGRSQ HQAYAWLLVP SLKDIKSDAK
     KRIDAITSIE SFGSCFELAN RDLEIRGIGE ILGNNQSGHI TKIGFSLYMK LLMNAVRNIK
     NGYYKPLNDI INTYPKIELN VSNLLPDSYI KKVNHRLFFY NKIATSNNFL DLEKIRLTLC
     KNFGNLPNSG DYLIKIAKIR LISKKIGVKK IKSDVKGGYI EFFEDSKINI QNLLKEFKKE
     KNCWKFDTSN RLRFSKNFKN NSERIDWILN MLININN