ID L5NBQ0_9BACI Unreviewed; 751 AA.
AC L5NBQ0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=D479_04313 {ECO:0000313|EMBL:ELK48106.1};
OS Halobacillus sp. BAB-2008.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK48106.1, ECO:0000313|Proteomes:UP000010769};
RN [1] {ECO:0000313|EMBL:ELK48106.1, ECO:0000313|Proteomes:UP000010769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK48106.1,
RC ECO:0000313|Proteomes:UP000010769};
RX PubMed=23469348;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BAB-2008.";
RL Genome Announc. 1:E00222-12(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELK48106.1}.
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DR EMBL; ANPF01000013; ELK48106.1; -; Genomic_DNA.
DR RefSeq; WP_008634013.1; NZ_ANPF01000013.1.
DR AlphaFoldDB; L5NBQ0; -.
DR PATRIC; fig|1246484.3.peg.904; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000010769; Unassembled WGS sequence.
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 GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000010769}.
FT DOMAIN 37..334
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 335..595
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 751 AA; 86615 MW; 4BB984B28FEE754B CRC64;
MEEGTSAFFH LFFLAEYIEE RNTIMDFFTR MEEQTGVRLN DVQKQAVTHT NGPLLLLASP
GAGKTTTLNM KIGYLLLEER VRPEQILAVT FSKASARDME ERFDRFFSGM TDQKVHFSTI
HSFAYQVVRE VLRKRGEDFQ LIEGSVSEEE WKKGFDGPDV PLHKKFILKR LFEERNGAAI
TEEEMDELMT YISFVKNRMV EGKELESVDC TVKHASDIYL AYERFKKTGA EKRLLDFDDM
LTYGYQLLLE ENDILKKYQQ RFSYLLTDES QDNSVVQHEI IELLAKPQNN LCVVADDDQS
IFMWRGSDVT KLLQFEKAYP EGTVMTMAQN YRSSKEIVQA SNQFIKRNKN RFQKEMFTEN
PSGKPVEIKA LKNYEEQLNY VTEEIRKSGS AEEVAVLYRN NASAVPLADK LDRAGVSFYM
KDIDAKFFRH WVVEDILNFL RFSYNDGRVD VLDRIHTKFN GYISKKQVAF LKRAGGGSVF
DTLLDTDIPS YQEKNLKLAK KHFHAINEME PDKAIRTIRE KLGYDHALQK MVEKFGFQAE
QLFGILDTLE EIAQGLGSLK GFADRLKELE HLIQTSKFNK ETSPLTLTTF HSAKGLEFDK
VFMIDLINGV VPSKDDMERY RSQDQGPMEE AVRLFYVGMT RARKDLQLLT YSYKGNERVT
ESLFVMNVRR IIQPGGSTVK KRPKHADVDL SDERLLTLDE VEIGRRIVHK KFGTGIIKAY
GGDQIGIEFH GAGYKELMLA FCLENGLLQK E
//
