ID J2GMY4_9BACL Unreviewed; 721 AA.
AC J2GMY4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, 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};
DE Flags: Fragment;
GN ORFNames=PMI05_00581 {ECO:0000313|EMBL:EJL31625.1};
OS Brevibacillus sp. BC25.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1144308 {ECO:0000313|EMBL:EJL31625.1, ECO:0000313|Proteomes:UP000007278};
RN [1] {ECO:0000313|EMBL:EJL31625.1, ECO:0000313|Proteomes:UP000007278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC25 {ECO:0000313|EMBL:EJL31625.1,
RC ECO:0000313|Proteomes:UP000007278};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL31625.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIX01000014; EJL31625.1; -; Genomic_DNA.
DR RefSeq; WP_007716939.1; NZ_AKIX01000014.1.
DR AlphaFoldDB; J2GMY4; -.
DR PATRIC; fig|1144308.3.peg.569; -.
DR Proteomes; UP000007278; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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}.
FT DOMAIN 93..377
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 378..646
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 11..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EJL31625.1"
SQ SEQUENCE 721 AA; 83405 MW; 216171DCE552AD0E CRC64;
PATAFQAVLA ATVEKDHSDD NTKEPLAFST KEHSEASIDE ENTPTIGSFR LPKKRTIGTS
TTPPPPAPKP PVFRKRLMPK KTISHMAEQM RDQSLHPGQQ QAVHATEGPF LILAGAGSGK
TRVMTARTTH LISDLGVKPN QIMVVTFTTK AADEIRQRIA RQLPAGQARE LIAGTFHSIF
YRMLLHHQPE RWDQQRLLKK DWQKWRLMRE TGALLGHDDL ATLKETEITE ALGIISRWKN
EYIRPQEVAY REATNDAEKR AIQLYPLYEA TKKKHQWFDF DDMLIGCYEM LRDDPGLLRR
YQERITYVMV DEFQDINRIQ YETVKLLAAP QNNLCVIGDD DQSIYGFRGS DPQYILGFTK
DFPQASTFTL EVNYRSHSSI VSLGYSLIGH NRERWAKECQ SFHREEGDTY LFEPEDEEEQ
ASRIVDEIIH RREQGAILGE CAILYRTNES ARPILERLSE AGIPFHYTQE EDSFYQRQTV
RWTLNYLRLA LNPDDTDALK EILSTLYISA EMWNALRSQA IIEDKPILHV LPHLTQLKPY
QRKHMQQINE ILTACKDISP AQALELIYED GKLRDYLKKR AKDREDGRER WSDELQQILA
ASKRHATISD FLAYIDQMAR QEKEWRNMRP LPDEAVHVLS IHRAKGLEYD HVFLPDLVEG
ALPHEYTLDE LRKGGSGALE EERRLLYVAI TRARRSLCIG IPRERFGRKT RTSRFIAEMG
R
//
