ID K9AFR2_9STAP Unreviewed; 1170 AA.
AC K9AFR2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=C273_09989 {ECO:0000313|EMBL:EKU46159.1};
OS Staphylococcus massiliensis S46.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU46159.1, ECO:0000313|Proteomes:UP000009885};
RN [1] {ECO:0000313|EMBL:EKU46159.1, ECO:0000313|Proteomes:UP000009885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S46 {ECO:0000313|EMBL:EKU46159.1,
RC ECO:0000313|Proteomes:UP000009885};
RX PubMed=23929469;
RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT the Surface of Healthy Human Skin.";
RL Genome Announc. 1:e00553-13(2013).
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:EKU46159.1}.
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DR EMBL; AMSQ01000020; EKU46159.1; -; Genomic_DNA.
DR RefSeq; WP_009384578.1; NZ_AMSQ01000020.1.
DR AlphaFoldDB; K9AFR2; -.
DR STRING; 1229783.C273_09989; -.
DR PATRIC; fig|1229783.3.peg.1995; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000009885; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000009885}.
FT DOMAIN 635..796
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..971
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1170 AA; 133948 MW; 2A2EF40A19B7E40B CRC64;
MKSIIKEIIT NDKRFNELNE KLGRENLLIT GLTPAAKATI IAEKYLSDDK QMVVVTNNLY
QADKLEADLL QYVDDEELFK YPVQDIMTEE FSTQSPELMS ERVRTLTALT KHQKGLFVVP
LNGLNKLITP RDIWAAHQIQ LNIGDDIDLD GFLEKLVAMG YKRESVVSHI GEFSLRGGII
DIYPLIGSPV RIELFDTEVD SIRQIDVESQ RSSENLESVE ITTATDLVIR DEELKRVKPR
LEKAYQETRP KIDKSVRNDI KETYESLLLA QSTMFDHQVL RRLISFMYAE KATIMDYLSD
DALCVVDEYN RVKETESTLA VENEEFMQNL IESGKGFIGQ TFTDDDALNR FVKSRKISYF
TLFTASMSVK LEDTIKFSCK PVQQFYGQYD ILNSEFNRFI QQDYRVVVLA ETKTKQERIQ
SMLSEMHIPT LKDTTAEMMS EGHAIITEGS LSEGFELPYM HLVVVTEREL FKSKQKKRKK
RHKTMSNAEK IKSYQDLKVG DYVVHVHHGV GRYLGVETLE VGDVHRDYIK IQYKGTDQLF
VPVDQMEQVQ KYVGSEDKTP KLYKLGGSEW KKTKAKAQSS IEDIADELLE IYKEREQSVG
YQFGPDTEEQ QTFEMDFPYE LTPDQDKSIS EIKGDMEVNK PMDRLLCGDV GYGKTEVAVR
AAFKAVMEGK QVAFLVPTTI LAQQHYETLI ERMSDYPIDI ELMSRFRTTK EVNQTKEGLK
SGKVDIVVGT HKLLGKSVQY KDLGLLIVDE EQRFGVRHKE KIKALKANVD VLTLTATPIP
RTLHMSMLGV RDLSVIETPP ENRFPVQTYV LEQNANFIKE ALLRELSRDG QVFYLYNRVQ
SIYEKREQLQ MLVPDASIGV AHGQMTERDL EETMLDFING DYDILVTTTI IETGVDVPNA
NTLIIEEADR FGLSQLYQLR GRVGRSSRIG YAYFLHPQNK VLSETAEERL QAIKEFTELG
SGFKIAMRDL NIRGAGNLLG KQQHGFIDSV GFDLYSQMLE EAVNEKRGIK EVEETPDIEM
NLNLDAYLPG SYIKNEQAKI EIYKKLRTLE SIEQLRDVKD ELIDRFGEYP VEVERLLDSV
EIKIHAVHSG VLTISDKNKS IEITLSEKGT QDINGEQLFK ETVALGRQMK VGVKENKMQV
TLKKSKQWLD QLKFVVKTIE ESMAIPDEDA
//
