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Database: UniProt
Entry: A0A0S1XWE4_9BORD
LinkDB: A0A0S1XWE4_9BORD
Original site: A0A0S1XWE4_9BORD 
ID   A0A0S1XWE4_9BORD        Unreviewed;       771 AA.
AC   A0A0S1XWE4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ASB57_03745 {ECO:0000313|EMBL:ALM82189.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM82189.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM82189.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM82189.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) 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; CP013111; ALM82189.1; -; Genomic_DNA.
DR   RefSeq; WP_057650670.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1XWE4; -.
DR   STRING; 1746199.ASB57_03745; -.
DR   OrthoDB; 5905204at2; -.
DR   Proteomes; UP000064621; 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; 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|PROSITE-ProRule:PRU00560,
KW   ECO:0000313|EMBL:ALM82189.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          3..280
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          281..580
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   771 AA;  85279 MW;  014DC1AE96DEC5BB CRC64;
     MIEKLNPQQR EAVTLEPQHA LVLAGAGSGK TRVLITRMAW LIQNGQASPF GLLAVTFTNK
     AAREMLTRLT STLPINTRGL WVGTFHGLCN RLLRAHHRDA GLPQAFQILD TADQLAAIKR
     LLKANGIDDE KFPPRDVQRF INGAKEEGER PNDVEVWDAH RRRLVEIYQL YEAQCQREGV
     VDFPELLLRA YELLARNAPV REHYQRRFRH ILVDEFQDTN KLQYKWLRLL AGGGAFIFAV
     GDDDQSIYAF RGANVGNMAD FERDYAHGTV IRLEQNYRSY GHILDAANAL IDHNSGRLGK
     NLWTEQGEGE PIRVIEQPSD GMEAHWIVDE IRALVNDGRA RREIAVLYRS NAQSRVLEHS
     LFSSGIPYKV YGGLRFFERQ EIKHALAYLR LLANPDDDTS WMRVVNFPTR GIGARTLEQL
     ADAARSQDTS LCAAVARVPG KGGANLAQFA MLIQRMAEET RQLPLPELVE HVLHGSGLLD
     HYKGEREGAE RIENLNELIT AATVFSAEEN FEGLPAGLVP QNEPPVTDAA TGEVLPGAPA
     DGGLTPLAAF LSHAALEAGD NQAEAGQDAV QLMTVHAAKG LEFDAVFISG LEEGLFPHEN
     SLLEQSGQEE ERRLMYVAIT RARERLYLSL AQSRMLHGQT RYAMRSRFLT EIPEQHLKWL
     TPRTGGVSQG YGGNQGGGYG EDRWSGASRD AFGRKPTGMA APRTPRSVTT GVTVGDRQFR
     IGMGVRHARF GDGTIVGLSG SGQDAQAQIQ FRDVGTKTLA LGIAKLDVVA S
//
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