ID A0A191V2C9_9ACTN Unreviewed; 829 AA.
AC A0A191V2C9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=GCM10010220_37350 {ECO:0000313|EMBL:GGR81558.1},
GN Spa2297_20245 {ECO:0000313|EMBL:ANJ09087.1};
OS Streptomyces parvulus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ09087.1, ECO:0000313|Proteomes:UP000078468};
RN [1] {ECO:0000313|EMBL:ANJ09087.1, ECO:0000313|Proteomes:UP000078468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2297 {ECO:0000313|EMBL:ANJ09087.1,
RC ECO:0000313|Proteomes:UP000078468};
RA Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA Takahashi H., Shirai M.;
RT "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT Integrated Site-Specifically with Actinophage R4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGR81558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR81558.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGR81558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR81558.1};
RA Sun Q., Ohkuma M.;
RL Submitted (DEC-2022) 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 ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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DR EMBL; CP015866; ANJ09087.1; -; Genomic_DNA.
DR EMBL; BMRX01000009; GGR81558.1; -; Genomic_DNA.
DR RefSeq; WP_064729417.1; NZ_JAMOLM010000069.1.
DR AlphaFoldDB; A0A191V2C9; -.
DR KEGG; spav:Spa2297_20245; -.
DR Proteomes; UP000078468; Chromosome.
DR Proteomes; UP000645274; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; 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; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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}; DNA-binding {ECO:0000256|RuleBase:RU364053};
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 71..365
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 366..649
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 829 AA; 91134 MW; 7D5CD10A84083B8A CRC64;
MSSLFDDSFL ASLQTPRGHE EEPPPPPEDG HGPEPVPHDL FGGKFDAPPE RDRYYRDGAP
RPALDPAALL DGLNDNQRAA VVHSGSPLLI VAGAGSGKTR VLTHRIAHLL AERGVHPGQI
LAITFTNKAA GEMKERVEQL VGPRANAMWV MTFHSACVRI LRRESKRLGF TSSFSIYDAA
DSKRLMALVC RDLDLDPKRF PPKSFSAKIS NLKNELIDEE DFAAQAADGF EKTLAQAYAL
YQSRLREANA LDFDDLIMTT VNLLRAFPDV AEHYRRRFRH VLVDEYQDTN HAQYALVREL
VGGAFEHPVD VPPEAEVPPA ELCVVGDADQ SIYAFRGATI RNILQFEEDY PDATTILLEQ
NYRSTQTILT AANAVIERNE SRRPKNLWTN QGAGAQITGY VADTEHDEAQ FVADEIDRLT
DAGEAKAGDV AVFYRTNAQS RVFEEVFIRT GLPYKVVGGV RFYERKEVRD VLAYLRVLAN
PEDSVPLRRI LNVPKRGIGD RAEAMIDALS QREKISFPQA LKRVDEAYGM AARSANAVKR
FNTLMEDLRT VVESGAGPAT VLEAILERTG YLAELQASTD PQDETRIENL QELAAVALEF
EQERAESEDA GTLADFLEQV ALVADSDQIP DEEDGGGVVT LMTLHTAKGL EFPVVFLTGM
EDGVFPHMRA LGQAKELEEE RRLAYVGITR ARERLYLTRS TLRSAWGQPS YNPPSRFLEE
IPAPHLEWKR TGSTGPAPSA PVSGVAASLS SSRSRSSASG ASGFATRRAA GAEQPTVSLA
IGDRVTHDQF GLGTVVGVKG TGSNAEATID FGDTKPKRLL LRYAPVEKL
//
