ID MFD_STAS1 Reviewed; 1170 AA.
AC Q49V12;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 132.
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=SSP2253;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008934; BAE19398.1; -; Genomic_DNA.
DR RefSeq; WP_011303869.1; NZ_MTGA01000029.1.
DR AlphaFoldDB; Q49V12; -.
DR SMR; Q49V12; -.
DR KEGG; ssp:SSP2253; -.
DR PATRIC; fig|342451.11.peg.2244; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006371; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
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; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 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; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 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..1170
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000282679"
FT DOMAIN 635..796
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 810..971
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 749..752
FT /note="DEEQ box"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1170 AA; 134754 MW; F1FD0CDED51E18E9 CRC64;
MKSIITEYIN EDKRYQELNE VFGKENVLVT GLSGAAKATI IAEKYLNSEQ QLLVVTNNLY
QADKLESDLL QFVEDSEIYK YPMQDIMTEE FSTQSPQFMS ERVRTLTALA QEERGLFIVP
LNGLKKWLTP VDMWKSHQLT LNVGDDIDID EFLNKLVNMG YRRESVVSHI GEFSLRGGIV
DIYPLIGKPV RIEFFDTEVD SIRDFDVESQ RSEGNIEHVD ITTASDYIIT EDVLKHTKHK
LKQAYEDTRP KIEKSVRNEL KETYESFQLF EAEMFDHQVL RRLVAFMYEQ PATIMDYFKE
DAIIAVDEYN RIKETETTLV TEIDEFMQNL IESGKGFIDQ SFLQYEGFEN LLKPFAVTYF
TLFTATMPVQ LNEIIKFSCK PVQQFYGQYD IMRSEFQRFI QNDYTIVVLA ETETKKERIQ
SMLNEMHIPT FIDTPSRRNE GGSAIITEGS LSEGFELPYM QLVVVTEREL FKSKQKKKPK
QHKTLTNAEK IKSYQDLKVG DYVVHVHHGV GRYLGVETLE VGGVHKDYIK LQYKGTDQLF
VPVDQMDQVQ KYVASEDKSP KLNKLGGTEW KKTKAKVQQS VEDMADELIE LYKAREMSVG
YKFGPDTAEQ NDFEIDFPYE LTPDQSKSIE EIKQDMEIER PMDRLLCGDV GYGKTEVAVR
AAFKAVMEGK QVAFLVPTTI LAQQHYETLI ERMQDFPIEV QLISRFRTTK EVKETKEGLK
SGFVDIVVGT HKLLGKDIQY KDLGLLIVDE EQRFGVRHKE RIKSLKNNVD VLTLTATPIP
RTLHMSMLGV RDLSVIETPP ENRFPVQTYV LEQNTNFIKE ALERELSRDG QVFYLYNKVQ
SIYEKREQLQ MLMPDANIGV AHGQMNERDL EETMLSFINH EYDIIVTTTI IETGVDVPNA
NTLIIEDADR FGLSQLYQLR GRVGRSSRIG YAYFLHPTNK VLSETAEDRL QAIKEFTELG
SGFKIAMRDL NIRGAGNLLG KQQHGFIDSV GFDLYSQMLE EAVNEKRGIK AEKQDAPEIE
IELNIDAYLP AEYIPNEQSK IEIYKKLRKI ESETQLMDVK DELIDRFNDY PIEVERLLEM
MEIKVHALHA GVTLIKDVGK QVEVYLSEKG TTDINGETLF KQTQPLGRTM KVGVQEGKMK
VTLNKTGNWL DSLKFLTKSL EESMVITDEI
//
