ID A0A140DWD9_9FIRM Unreviewed; 716 AA.
AC A0A140DWD9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AALO17_18320 {ECO:0000313|EMBL:AMK54966.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK54966.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK54966.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK54966.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP011391; AMK54966.1; -; Genomic_DNA.
DR RefSeq; WP_067558046.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DWD9; -.
DR STRING; 1702221.AALO17_18320; -.
DR GeneID; 78478471; -.
DR KEGG; fro:AALO17_18320; -.
DR PATRIC; fig|1702221.3.peg.1787; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000069771; 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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:AMK54966.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:AMK54966.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000069771}.
FT DOMAIN 6..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 281..555
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 636..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..525
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 641..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 716 AA; 81515 MW; 57FB5A2B0F837619 CRC64;
MSSVIDSLNA PQKEAALTLD KDVRIIAGAG SGKTRMLMAR IASLVDNGIL PWRILAITFT
NKAAREMKER LQTLLQDAAR DVRISTIHSL CVRILREDAS AIGYPKNFTI LDGDDQKSML
RTIYKELDMD RTTFPPSAVL GKISGWKTAG YSPEEAQDQT DGPEAKAYEL YERQLEDMKA
MDFDDLLLKT RHLLGTNQEV RDKWQNRLDY IHVDEFQDVD PVQYDIIRLL KRPDAFLCVV
GDPDQTIYTW RGAAVDIILN FARDFPNTRT VILNENYRSS QTILDAANAL IAHNHGRIEK
DLFSSIESDR KIETFQAQDE SQEPLQVARD ITRARKEGLE YRDIAVLYRS NYLSRGIERV
LGKLRIPYRI YGGIRFYERQ EIKDMLSYLK LITEPDPEDP AQKSLDLAVM RVINVPRRGI
GARTVEKLQK EAADRGLNLL EVLRDPQTVS GAAAKKFAPF VELVDEMKSL RASVPLDELM
MRMAFDSGYM AMLKDTREED REENIEELQA DIRQALQENP DLTLEEYLQD LSLFTDRDEE
AGNAVSLMTV HAAKGLEFEQ VHIVGLNEGV FPSLRAMEEA GRDGLEEERR LMYVAMTRAK
KALYLSWNSG YSFQLDRHKT PSRFIQEIPE DYVKQESTPL DNYPVHKSPQ GQSRKSRGRA
PKPTTRLRKG DHVEHTVYGA GVVTDVQKDI VSVAFGHPNG VRKLNMHHPS LQKVKG
//