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Database: UniProt
Entry: A0A140DWD9_9FIRM
LinkDB: A0A140DWD9_9FIRM
Original site: A0A140DWD9_9FIRM 
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
//
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