ID A0A0S1Y6Q2_9BORD Unreviewed; 755 AA.
AC A0A0S1Y6Q2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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_24965 {ECO:0000313|EMBL:ALM85772.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM85772.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM85772.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM85772.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013111; ALM85772.1; -; Genomic_DNA.
DR RefSeq; WP_057654621.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y6Q2; -.
DR STRING; 1746199.ASB57_24965; -.
DR OrthoDB; 9792687at2; -.
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 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; IPR043764; DUF5710.
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; PF18974; DUF5710; 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:ALM85772.1};
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 15..320
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 320..593
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 680..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 755 AA; 83233 MW; 6C9A6934D35FDCBC CRC64;
MTTDSPAPQF IPAGLVPTSE QRDIQLARQR ISLVQANAGA AKTTTLALRV GEALARGLAP
QAILALTFTV EARQVMRARL LDVGLPAATV AQLTVLTLDE LAQRVLARLE DDAPAQLLSA
RDLKQPALDA LDGLAEAYPS YVDQLEIRTH DSAVSQFLDN LLNLKARLAL DLGDRDEEQS
LAYVAEDRGI ALTDLLWAQE FERLRQGGGE TPQFRGPWDA TYDLARLLRD FPECADALPV
YRLVVADELH DVNEAAYTVL ETLLAGADHG REAVYFVGAG DRDQVIHSRL GADEQYLDRR
FAARFPATVN YPLTVTWRHG PHLAHAMEAF KRKPVRSGLP VKTDLDVMLY AADQPPAAGC
AGQVIAALTR WKADRHPLDG CAILLRDRHQ SIAIENALMQ ADIGYRTQTM PSYLRREEIL
FLRGMLAIAL DNLHTVEAMP VREDIVAALA LFGEVPLTPE ELMQAKRDIA KQPELLKTFF
QYQIQRVGAE AARRRMAAAV DHVRGLPDDA PAHEALLRIC EEVAVENLAQ RLYVHPYDTE
VVTRSVQGFV AAARDSGRSL RDFANWIGTA DAFVAARRSK NLVLLECVES AKGKEFDHVI
LPFLEIGEFP HPLRAAREEE NLFYVAATRA RARLTLIAPA AEPLRSPYIA RMEITATRAR
SDAAVQTNLA ARQAKAAAQA NANAVTQTPT SARARASAPA RGTPADSGRR ELKVSYADKE
HVKKLGARWD PTRKIWYAPE GVDIEPLRPW LPPGH
//