ID Q7VY15_BORPE Unreviewed; 1134 AA.
AC Q7VY15;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 OrderedLocusNames=BP1548 {ECO:0000313|EMBL:CAE41838.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41838.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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};
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DR EMBL; BX640415; CAE41838.1; -; Genomic_DNA.
DR RefSeq; NP_880284.1; NC_002929.2.
DR RefSeq; WP_010930421.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VY15; -.
DR STRING; 257313.BP1548; -.
DR PaxDb; 257313-BP1548; -.
DR GeneID; 69601467; -.
DR KEGG; bpe:BP1548; -.
DR PATRIC; fig|257313.5.peg.1661; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_009270_0_0_4; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000002676}.
FT DOMAIN 7..483
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 495..790
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1134 AA; 122174 MW; C11D39ED446DD6D5 CRC64;
MTEPERLPHD HAARRQALDP SRSFLVQAPA GSGKTELLTD RILALLATVT RPEEIVAITF
TRKAASEMHA RVLHKLSLGA GEPPRSAHER RSWELARAAL ARDQEQGWHL LDHPARLAIR
TIDSFCAGLV RGMPWLSELG GMPDIADDAR AHYEAAARAT LELADEHDAV RALLAHLDVD
VQAAKDAIAA MLGQRDQWMP LLQFGLDRDG LEASLAEALE HELDSLCGQL PRGWSQALCG
PARLAAAALA GSGDARLAAL QDWDAPLPPM AEALDQWRAL AHLLLTGTGA LRSPKGVNKN
LGFPAGCDHK EPFTAWLAAC DGGAPWVRAL AAVRDMPDAH FSDAQWDVLS AQLTTLALSV
AQLRVQFARA GEVDFIEIAQ RAAYALGSGD DPGELLLKLD ASIRHLLIDE FQDTSQGQID
LLATLTAGWQ DGDGRTLFLV GDPMQSIYRF RKAEVGLFLQ VAERGVGQIR PGFLQLTDNF
RSQGGVVDWV NRVFAQLLPR ANDADSGAIA YSPSTAFHET APGEAVLFHP AWECGDAASA
ERQAEDIAVG LVRAALAEHE GSRHPVAILV RARSHLGSLT RRLAQEGIPC RAVELVPLGL
RPVVADLVQL ARALAHPGDR LAWLSVLRAP WCGLTLTSLQ RLFGADQLTP VPTLLERALR
GAARSEGGQG SLFDAPAPGC LAEQALAPDE YRRLRAVAAI LLDRANDAGL LPLAAWLEQL
WRRLGGPGLY AGSSAASDAE SLFQLIERLA PHGGLDAGLL DTAVARLFAA PQATGEQGTV
EIMTMHKSKG LQFDTVILYG LHRAPRGDQA PLVRFEQSRG RVLLGPIKPR AETEADPVSR
YLGAREARRA AYETDRLFYV AATRARQRLH LVAHVAVDAA SGQARTPASA SLLGRLWPHL
SVPQPPDVAQ DQAAATGEQP ALVGEPLRRL AGAGLASLAA RTLPREAAAG VYGGGQGAEH
PSWQLEAGYD AAVGTLAHAW LARIGGDGPQ HWSADALAVR LPAMRRQLTR AGIPAGQADA
AAQAVLDTLQ STLDDERGRW LLGQARARRE WPLIDAAGRV SVIDLALSTE DGWLIVDYKT
GRPHEHETPE QFAIRMRQRH GEQLMRYCAQ VTALDGRPAR AALYFPRARA WIDL
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