ID A0A150N8Y7_9BACI Unreviewed; 701 AA.
AC A0A150N8Y7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=B4110_3555 {ECO:0000313|EMBL:KYD33082.1};
OS Parageobacillus toebii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD33082.1, ECO:0000313|Proteomes:UP000075324};
RN [1] {ECO:0000313|EMBL:KYD33082.1, ECO:0000313|Proteomes:UP000075324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4110 {ECO:0000313|EMBL:KYD33082.1,
RC ECO:0000313|Proteomes:UP000075324};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-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:KYD33082.1}.
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DR EMBL; LQYW01000002; KYD33082.1; -; Genomic_DNA.
DR RefSeq; WP_062677064.1; NZ_LQYW01000002.1.
DR AlphaFoldDB; A0A150N8Y7; -.
DR PATRIC; fig|153151.4.peg.680; -.
DR Proteomes; UP000075324; 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}.
FT DOMAIN 58..332
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 333..612
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 701 AA; 82165 MW; CA94AFA9BA6BDC1D CRC64;
MKLFNPFYKK PINFHKKPIN SRKEIPIAEV LNPLTTKQLV KENDHDQFYF RMLEQQGIVL
NERQLEAVRQ TEGPVLTLAG AGSGKTSVLT ARIGYLINVK KVKPENILVL TFTRKAAEEM
KERIAQLPGL SKNTVRNLVA GTFHSVFLQI LKSQGYDHRI LSNEKHKEVI IKRILKDMGL
KDDYEPETIL SLISYSKNQL LTIEDLPEQT PVEREFKDIF RRYEEWKNKE HCMDFDDMLV
YTYQLLNENQ RLLERLQERF KYIEVDEFQD TNIAQYRVLQ MLAEKHKNLF VVGDDDQSIY
AFRGASSDII LNFPKDYPNT RIVKLDINYR SNPSIVGLGN EIIKYNQKRH AKTLRCYKRS
NEYLTPFYMR PKDTADEAQL IVENMRSDVQ QGTRKWKDFV VLYRTHAVSR AIVEQLVLKN
IPFVVYGDKK PFYEHPIVKP VLDYIRLSIN PNHLNALKSI LPTMYLNRDK AIDYITTEMV
FNPLDESKTL LHYLLRMPGL HPSQKELIIE RIRLLDDIKK MSPVDAIREI RQGKGQYEKY
LEIDQRRSFT LQKEFANEML DELVSSAIPH KTHESYLNLI DKILKKHEEM EELKKDPYAD
VVSLMTIHNA KGLEFPCVYL IGASDYILPH AVAIQGAEDI ITTQQKHNKS KNTSVNEAIE
EERRLMYVAV TRAKEELYIS SPKTFRNRDL EISRFLLEVF R
//
