ID A0A0M2STG9_9BACI Unreviewed; 761 AA.
AC A0A0M2STG9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=WQ57_16600 {ECO:0000313|EMBL:KKK37001.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK37001.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK37001.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK37001.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-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 -!- 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:KKK37001.1}.
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DR EMBL; LAYY01000019; KKK37001.1; -; Genomic_DNA.
DR RefSeq; WP_046524885.1; NZ_LAYY01000019.1.
DR AlphaFoldDB; A0A0M2STG9; -.
DR PATRIC; fig|1408103.3.peg.3694; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000034166; 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:UP000034166}.
FT DOMAIN 137..416
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 417..684
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 761 AA; 87120 MW; FDD53F9AB2D651EB CRC64;
MQTAYYKEKI INLPGIRRED FQKLYEDGKK GLLSCPVCGA PVRLYLGIHN RPHFYHHLSK
AAACSDLPIQ DAAEEHPEHT EWGGFRLPTA RGITAEEKEV AYKPSQALRI KRPFTKKPVL
SSEKQDSYIE KLKDAGISFD SNQQTAVTHT EGPLLILAGA GSGKTRVLTA RTAYILKQLK
VPANSMMLVT FTAKAAGEMK KRLIGYPGVY QDEAQRIVSG TFHSIFYKIL LHHNRDKWSG
EHLLKKDWQR EQIVKDAGRT LSLDEKEFAY DLALQQIGLW KNSMILPKGV KPQSSWEEKT
ALLYQHYEET KDRSGLFDFD DMLLGCHSLF VDEPQLLESY QNRFTYFLID EFQDINKVQY
ELIKMLSART NNVCAVGDDD QSIYAFRGSD PSYLLEFERD FPGAEVVTLN QNYRSPHEIV
ETANSIIAGN TKRHQKEMKA QYSHEIKPML FYPFDEEEEA TMILTDLQEK IEQGAKPSHF
AILFRTNTGS RAMFERLASS SLPFKLEQDN ESFYERFMVR GLLAYFRLAI NEDDSEAVRS
ILPSLFLKQS VFRDLQAESI LKDCSMLEAL SHVKTGFAFQ EQKLKKLVPM VRSLAMLSPL
AAIERVEKEL GYQDFIKKRG SEGNKMEKGS DDIRDLRVAA RKFKNISELI DHADHMTAMN
KEIKVLGKRH DDAVILSTIH RSKGLEYKYV YVLGAVDGSL PHDYALDSAR NGDLLPLEEE
RRLLYVAVTR AMEQLFISVP IYRRGRKAHP SRFLTQLPKI Q
//
