ID A0A0R1RLQ3_9LACO Unreviewed; 1180 AA.
AC A0A0R1RLQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN ORFNames=FC70_GL000032 {ECO:0000313|EMBL:KRL58144.1};
OS Paucilactobacillus oligofermentans DSM 15707 = LMG 22743.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423778 {ECO:0000313|EMBL:KRL58144.1, ECO:0000313|Proteomes:UP000051697};
RN [1] {ECO:0000313|EMBL:KRL58144.1, ECO:0000313|Proteomes:UP000051697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15707 {ECO:0000313|EMBL:KRL58144.1,
RC ECO:0000313|Proteomes:UP000051697};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL58144.1}.
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DR EMBL; AZFE01000001; KRL58144.1; -; Genomic_DNA.
DR RefSeq; WP_057888999.1; NZ_LN898144.1.
DR AlphaFoldDB; A0A0R1RLQ3; -.
DR STRING; 1423778.FC70_GL000032; -.
DR KEGG; lol:LACOL_1515; -.
DR PATRIC; fig|1423778.4.peg.41; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051697; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000051697}.
FT DOMAIN 634..795
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 816..970
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1180 AA; 133221 MW; 50E420952B50B3CF CRC64;
MKLEDFLVEM PEFINIEAGI KGRQRQLITG ISGSAETLLL SSIHRQLQQS QLIVTDDLSH
MEQITNDLLN RLSDDQVFQF PVEENLAVEV ATSSPEFRLQ RVLALDALLS DHPVVVVTST
SGLKRLLPTT EVFKEARLQI KVGSDINLDQ SRTQLSSMGY QLEKMVIRPG DFAIRGSILD
IYPLNTENPV RIDLFDTEVD SLRYFDATTQ RSIENVEQVS VLPATDFVIS ETEFNRIHQS
LTKQMTATAK DLSDDQRQQL EQNISPTLKA LTHQQIIPEL IEFSNDVYTD KTSILDYLDE
NGVIVTEDYP RILTKEEDIN EGQQAWLEAQ VASQKLLSST AMGHKVSDLI TGDQHAQCFF
ALFQKGMGKV SFSQITNIMA RNMQQFFGQM PVLKAEIERF NQQQRTTIIL ANSADRLDKI
ENTLNDFGIS ITLVENDELK PGIAQLVNDG LQNGFELPEA NLVVITEAEL FKTVQKKRAR
RQTLENAERI KSYTDLKPGD YVVHVNHGIG QFTGIETIES QGVKQDYIAI EFQKNAKIFV
PVTQLNLVQK YVSSESKTPK INKLGGSEWA KTKRSVAAKI EDIAQELVAL YAAREAEVGF
NFPKDDDYQN QFENDFPYTE TPDQLRSSSE IKRDMEGTKP MDRLLVGDVG YGKTEVALRA
AFKAIEAGKQ VAFLVPTTIL AQQHFDSMQR RFEGYPVNVA MMSRFRTRKQ LTETEEQLTS
GECDIVVGTH RILSKDVHFK DLGLVIVDEE QRFGVKHKER LKQLKSSVDV LTLTATPIPR
TLHMSMLGVR DLSVIETPPV GRFPIQTYVM EQNAGALRDA VMREMGRGGQ VFYLHNRVAD
IEKTVAEISM LVPEARVGYI HGQMTEVQLE SVLYDFIRGE YDVLVTTSII ETGVDIPNVN
TLFVEDADRM GLSQLYQIRG RIGRSNRVAY AYFMYQQNKV LTEVSEKRLS AIRDFTELGS
GFKIAMRDLS IRGAGNLLGQ QQHGFIDSVG YDLYSQMLAD AVAVKRGEKV VVKTDTEIDV
GIEAYLPSEY IDDQRQKMEL YKSIRSLESE DRLLDLESDL IDRFGDFPVQ VENLLAVGRL
KIFADLAQLD KIRQQNGYLY VTLSENATEK ITARELLKDL TVTGFKATIG DEAGKTRIKL
VIQPKMTQKD WMEQLTVFVK ALSEHFEGPG EQNDEESTTA
//
