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Database: UniProt
Entry: N1ZMU7_9LACO
LinkDB: N1ZMU7_9LACO
Original site: N1ZMU7_9LACO 
ID   N1ZMU7_9LACO            Unreviewed;      1164 AA.
AC   N1ZMU7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=C821_01484 {ECO:0000313|EMBL:EMZ18322.1};
OS   Lactobacillus sp. ASF360.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=97137 {ECO:0000313|EMBL:EMZ18322.1, ECO:0000313|Proteomes:UP000012594};
RN   [1] {ECO:0000313|EMBL:EMZ18322.1, ECO:0000313|Proteomes:UP000012594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF360 {ECO:0000313|EMBL:EMZ18322.1,
RC   ECO:0000313|Proteomes:UP000012594};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
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:EMZ18322.1}.
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DR   EMBL; AQFR01000131; EMZ18322.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1ZMU7; -.
DR   STRING; 97137.C821_01484; -.
DR   PATRIC; fig|97137.3.peg.1337; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_9; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000012594; 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}.
FT   DOMAIN          629..790
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          807..965
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1164 AA;  133241 MW;  78436ADD8759C506 CRC64;
     MRLTNYLEKD KDLNNFIDKT KDVKNSMITG ANAGAFSLLL KQIVNERKAP LVLIEENEHK
     AQDLYGKLSA ILPEGQVQIF PVDDMIATQT ATTSPDELSS RIQTLNFLLS NKPGIVVTTP
     AGLQYKLSKP EEYLAFKKTF DLDSEYDLKE LNDWLVRAGY HKESLVGKSG EFAIRGDILD
     IYPLDRENPV RIEFFGDEID SIKEFDLSTQ RSQKELDKLT IFAAHDRVFS RDNLKKAAEK
     IRKAMANAPA PEKAVKDHFT QSLDELDAGG LPNNYAFLVD YLISRPSSLL EYLSKDGLVF
     LDDWPLINQS VKNVDSENAA FIDDELKTGA MLPGQELRLN FKRVWSKDSH HRIYFSLFQR
     SLGRIKLDQM LDWQTREPEQ FFSQMPLIKT EIESYQKNAQ TVILQADNEK RAKQMSQNFA
     DFGLDIPIVN KDDLIEKRTQ IVVGEFSEGF NLPNINLIYL TERELFNKRV HHKKRIKTLE
     NAQRLRNYTE LKPGDYVVHV NHGIGRFEGI KTLENNGVKR DYITITYQRG DQLFVPADQL
     KLVQKYVGSE GKRPHLNKLG GSEWAKTKRK VQSKVEDIAD DLIELYAKRE SEKGFAFSPD
     DDLQRQFESA FPYVETADQL RSTKEIKEDM ESSKPMDRLV VGDVGFGKTE VALRAAFKAV
     QDNKQVAFLV PTTILAQQHY ETILDRFKDF PVNVAMLSRF QTPAETKEII EKLKKGEIDI
     VVGTHRILSK DVEFKNLGLL IIDEEQRFGV KHKERLKQLK ANIDVLTLTA TPIPRTLHMS
     MVGVRDLSVM ETPPQNRYPI QTYVMEELPS VVKNACQREM QRGGQVFYLH NRIGDIDEVV
     NKLEKLMPNA RIASIHGRMS QNQIEDILYR FLNREFDILV TTTIIETGID MPNVNTMIIE
     DADKYGLSQL YQLRGRIGRS ARLAYAYFLY QPNKVLTEVG EKRLDAIRDF TELGSGFKIA
     MRDLSIRGAG NMLGSQQHGF IDSVGYDLYS QMLSDAIKAR KNKKVIKKSN SEIDLGFESY
     IPDAYIPDQE EKIEFYKKIK AVTSEEELDQ IEDELIDRFG DYPTSVENLL ASSKLKLNAD
     NAQALNVVKK DDKIKVEFDI KASKELEGPN IFKALEHVSF KARISMTKDK KMVVLLLLPD
     KLNNRMLFNE LTTFLEDASE IVQK
//
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