ID F8C4U1_THEGP Unreviewed; 701 AA.
AC F8C4U1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=TOPB45_1355 {ECO:0000313|EMBL:AEH23436.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23436.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH23436.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH23436.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP002829; AEH23436.1; -; Genomic_DNA.
DR RefSeq; WP_013910134.1; NC_015682.1.
DR AlphaFoldDB; F8C4U1; -.
DR STRING; 795359.TOPB45_1355; -.
DR KEGG; top:TOPB45_1355; -.
DR PATRIC; fig|795359.3.peg.1376; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_10_0; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006583; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF3; ATP-DEPENDENT HELICASE_DEOXYRIBONUCLEASE SUBUNIT B; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000006583}.
FT DOMAIN 8..292
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 293..555
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 701 AA; 81808 MW; DE1BE3385A74963F CRC64;
MKNLEFLKEL NPAQAEAVRT IFGPLLVIAG AGSGKTKTII CRMAYLVAHG VPPEKILLLT
FTRKAGKEMI ERAGALLKMD CNKIMGGTFH SLCQYMLRFY GYLLGYKPNF TILDRSDSED
LINLLRNSLG LAERKKRFPK KDTLASIYSK MINQQKTLEE ILSHEYPQFL DHYYEIERLF
IEYVNYKKEH QLMDYDDLLL NWLEVLKNFP EVRKEIGKKF EFIMVDEYQD TNFLQGEIIK
YMGETHKNVM VVGDDSQSIY GFRGAYFRNI FEFPKLFPDT KIIKLEQNYR STQSILDLAN
VIISNSKIKY TKTLFTLKKG GRKPVLFKAK DETESSKFVA DKVLEFRENG IKLSQMAVLF
RSAYHSFDLE VELTKRGIPF VKYGGLKLLE SAHMKDFLSL LRIISNPQDF ISWHRVLLLL
EGIGPKSTEK IISSLKQNLL NIDYTLEKLI FQFPQKEFKE LVILLKELWK NKKSLSEILI
SVWDFYKPIF ERIYYEDYHK REKDIEGVIA LSEKYNLLED FLTDLILEPI EVTDIEKPAK
DEDCLTLSTV HSAKGLEWHT VFIISLIEGR FPSAYSIHND EELEEERRLF YVAVTRAREN
LFLIAPMTIY IPGEGKTLAK LSRFIKEVPP SLLEFYKEEE FKEKELDNGK KFKVGDIVKH
PHFGIGEVRE ILSSEKIRVF FEEKGNTLLN LKYTNLEKLI M
//