ID A0A1S2QYG8_9BACI Unreviewed; 769 AA.
AC A0A1S2QYG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BIV60_18655 {ECO:0000313|EMBL:OIK11174.1};
OS Bacillus sp. MUM 116.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK11174.1, ECO:0000313|Proteomes:UP000180019};
RN [1] {ECO:0000313|EMBL:OIK11174.1, ECO:0000313|Proteomes:UP000180019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 116 {ECO:0000313|EMBL:OIK11174.1,
RC ECO:0000313|Proteomes:UP000180019};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 116.";
RL Submitted (OCT-2016) 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 -!- 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:OIK11174.1}.
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DR EMBL; MLYR01000081; OIK11174.1; -; Genomic_DNA.
DR RefSeq; WP_071357216.1; NZ_MLYR01000081.1.
DR AlphaFoldDB; A0A1S2QYG8; -.
DR STRING; 1678002.BIV60_18655; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000180019; 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 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; 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:UP000180019}.
FT DOMAIN 139..418
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 419..686
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 749..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 769 AA; 87997 MW; 2A9512BFD7EB8FF1 CRC64;
METAIYQNQT ISLDSLDRSE YQKIYLAGKN GELLCSVCRE SVRFYIGIQD SPHFSHAHST
IPDCPEQTIQ EVNNEPEQNH NEMNGFRLPK GRSILAAPEK VQAFKTAKSL DYQVPFQNIE
TNTIEYPSPY LQQLAKSGVV LDDAQAAAVS ETEGALLVLA GAGSGKTRVL TARTAYMLEV
QKIDPRNIML VTFTSKAASE MKNRLLTYPQ IKKEAINKLV TGTFHSIFYR ILMFHSRENW
NSERLLNKDW QRDKILKNAG KEIGLSEKEF AYDLALQQIG FWKNSLLFPE DIHPESEWEK
QTLYLYKKYE DYKLAERLFD FDDMLIGCYQ LLKSTPELLE QYQNRFQYFL IDEFQDINKV
QYELIKLLSG KYKNVCAVGD DDQAIYSFRG SDPSYLLDFE KDFPSAKVIT LAENYRSSHE
IVTAANQMIA ANKKRRLKKM KAQYTHGAAP IIFFPYDEEE EATMIVTDLQ KKIAQGAAPS
DFAILYRTNA GARAVFERLA SSNLPFRIEQ DVEAFYDRRI VKSILSFLKL SLNEDDQTAL
SDVLPYLFLK QAVLRDLKAM SILQDCSNLE ALSYIKTAHS FQEKKLKQAV TAIRKLKQLT
PLSAIEMIEK DIGFLDFLKK RGNESNMLEK GSDDIKDLKV AAKNFNSIES LLAHAEHMSA
MNKEIKNLSK HFTETITLST IHRAKGLEYQ TVYVLGAVDG SLPHDFALES YRNGDYSALE
EERRLFYVAM TRAKEQLFIS IPSNRRGKKA NRSRFLTSLS KKRNRPASL
//
