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Database: UniProt
Entry: A0A1W6YP93_9BORD
LinkDB: A0A1W6YP93_9BORD
Original site: A0A1W6YP93_9BORD 
ID   A0A1W6YP93_9BORD        Unreviewed;       765 AA.
AC   A0A1W6YP93;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE   AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN   ORFNames=CAL12_17260 {ECO:0000313|EMBL:ARP82393.1};
OS   Bordetella genomosp. 8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP82393.1, ECO:0000313|Proteomes:UP000194151};
RN   [1] {ECO:0000313|EMBL:ARP82393.1, ECO:0000313|Proteomes:UP000194151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU19157 {ECO:0000313|EMBL:ARP82393.1,
RC   ECO:0000313|Proteomes:UP000194151};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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; CP021108; ARP82393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YP93; -.
DR   STRING; 1416806.CAL12_17260; -.
DR   OrthoDB; 5905204at2; -.
DR   Proteomes; UP000194151; 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   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; PF21196; PcrA_UvrD_tudor; 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}.
FT   DOMAIN          3..280
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          281..581
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          682..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   765 AA;  84615 MW;  6B50AD52ECE63504 CRC64;
     MIDKLNPEQR AAVTLEPQHA LVLAGAGSGK TRVLTTRMAW LIQNGLASPY ALLAVTFTNK
     AAREMLARIT AILPIDTRGL WVGTFHGLCN RLLRAHHRDA GLPQAFQILD TADQLAAIKR
     LLKANGIDDE KYPPRDVQRF INGAKEEGQR PGELEAWDSH RRRLIEIYQL YEAQCQREGV
     VDFPELLLRA YELLSRNAPV REHYQRRFRH ILVDEFQDTN TLQYKWLRLL AGGGAHIFAV
     GDDDQSIYAF RGANVGNMAD FERDYAHGTV IRLEQNYRSY GHILDAANAL IDHNSGRLGK
     NLWTEQGEGE PVRVIEQPSD GMEAQWVVDE IRALVNDGRA RREIAVLYRS NAQSRVLEHA
     LFSAAIPYKV YGGLRFFERQ EIKHALAYLR LIANPHDDTS WMRVVNFPAR GIGARTLEQL
     ADAARAHDTS LYGAVARVAG KGGANLAQFA ALIGRMADDT RELPLPEMVE HVLEASGLIE
     HYRGEKEGTE RIENLNELVN AAAVFSTEEN FDGLPAGVAA QREPIPGPDA AGATDPAFAA
     PAENLTPLAA FLSHAALEAG DNQAQAGQDA VQMMTVHAAK GLEFDAVFIT GLEEGLFPHE
     NSVLEQAGLE EERRLMYVAI TRARERLYLS LAQSRMLHGQ TRYAMRSRFL GEIPEQHLKW
     LTPRATMGDE YGAANRDWRG ADRDAFGRKP TGTIAPRQPR GVASGVTVGD RQYRIGQGVR
     HARFGDGTII GLSGNGQDAQ AQIQFRDVGP KTLALGIAKL DVIAG
//
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