ID A0A0N7FUA8_9ACTN Unreviewed; 841 AA.
AC A0A0N7FUA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ACH46_04095 {ECO:0000313|EMBL:ALG83839.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG83839.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG83839.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG83839.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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}.
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DR EMBL; CP011853; ALG83839.1; -; Genomic_DNA.
DR RefSeq; WP_062391800.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N7FUA8; -.
DR STRING; 1136941.ACH46_04095; -.
DR KEGG; goq:ACH46_04095; -.
DR PATRIC; fig|1136941.3.peg.828; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000063789; Chromosome.
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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 22..315
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 316..644
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 581..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..602
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 841 AA; 91701 MW; 19C3AED5AAF36221 CRC64;
MNTSLAAATE TTLSDRGREL LDGLNPQQRE AVLHAGSPLL IVAGAGSGKT AVLTRRIAFL
LAERDVTPGQ ILAITFTNKA AAEMRERVID LVGPRAAYMW VSTFHSTCVR ILRAQSGLLG
NRNSNFSIYD ADDSRRLIGM VVRDLELDPK KFSPRGVGTQ ISNFKNELKD PDDAAAEAAA
EGNTDLTAGA IAQIYAEYQR RLAAANAFDF DDLIGETVSL LQRHPNVAEY YRRRFRHVLI
DEYQDTNHAQ YVLVRELVGE KVTESGLEPS ELCVVGDADQ SIYAFRGATI RNIEEFERDY
PDAETILLEQ NYRSTQTILS AANAVISRNA GRREKKLWTD SGDGDLIVGY VADSDRDESA
FIAKQIEELV DYSIGGSASH TYADVAVFYR TNTGSRSLEE VFVRHGIPYK VVGGTKFYER
KEVRDIVAYL RVVANPDDAV SLRRILNTPR RGIGDRAEAC VAVHAENLGI SFYQALVDAT
ENRVALLNTR AVKQITSFVN LIEGFRSDFL MAFGAVGGEQ VDDAVADATT EGADIGELVD
AIVDRSGYRA ELEGSNDPQD AARLDNLNEL IAVARDFSAE AAQAAEEAPD DETDEDGEIV
GDGEPEPGSL AAFLEKVSLV ADADQVPDEG EGVVTMMTLH TAKGLEFPVV FVTGWEDGHF
PHMRALGDPA ELSEERRLAY VGITRAREKL YLTRAMSRAS WGQPVSNPES RFLQEIPQHL
IDWRRTEPKR GMRDHGSRGG SFGFGSTRGG SSFGGSSFGG SDGGFGSGMR GRSSYSSDPT
RGRNKNVHYE IGDRMNHPQY GMGKAVAKEG SGVTERITFD FGGSVGRVTL MTVGGLPGEK
L
//
