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Entry: A0A0A7JV78_9PSED
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ID   A0A0A7JV78_9PSED        Unreviewed;       669 AA.
AC   A0A0A7JV78;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE            EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01920};
DE   AltName: Full=DNA 3'-5' helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   Name=rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   ORFNames=NJ69_18280 {ECO:0000313|EMBL:AIZ34809.1};
OS   Pseudomonas parafulva.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ34809.1, ECO:0000313|Proteomes:UP000030632};
RN   [1] {ECO:0000313|EMBL:AIZ34809.1, ECO:0000313|Proteomes:UP000030632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ34809.1,
RC   ECO:0000313|Proteomes:UP000030632};
RA   Liu Q.;
RT   "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT   bacterium isolated from rice field.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC       involved in DNA replication; it can initiate unwinding at a nick in the
CC       DNA. It binds to the single-stranded DNA and acts in a progressive
CC       fashion along the DNA in the 3' to 5' direction. {ECO:0000256|HAMAP-
CC       Rule:MF_01920}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01920};
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|HAMAP-Rule:MF_01920};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|HAMAP-Rule:MF_01920}.
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DR   EMBL; CP009747; AIZ34809.1; -; Genomic_DNA.
DR   RefSeq; WP_039581930.1; NZ_CP031641.1.
DR   AlphaFoldDB; A0A0A7JV78; -.
DR   KEGG; ppv:NJ69_18280; -.
DR   eggNOG; COG0210; Bacteria.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000030632; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01920; Helicase_Rep; 1.
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; IPR005752; Helicase_Rep.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR01074; rep; 1.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 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|HAMAP-
KW   Rule:MF_01920};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01920}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01920};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01920};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01920}.
FT   DOMAIN          2..280
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          281..563
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ   SEQUENCE   669 AA;  76791 MW;  69E0F7DC14B8F9D5 CRC64;
     MSRLNPRQQE ARDYVGGPLL VLAGAGSGKT SVITRKIAHL IQNCGIRAQY IVAMTFTNKA
     AREMKERVAT LLRPGEGRGL TVCTFHNLGL NIIRREHQRL GYKPGFSIFD ESDIKALLSD
     IMQKEYSGDD GLDEIKNMIG SWKNDLILPA EALEKARNPR EQTAAIVYTH YQRTLKAYNA
     VDFDDLILLP VKLFQEHPDV LDRWQNRVRY LLVDEYQDTN ASQYLLVKML IGLRNQFTVV
     GDDDQSIYAW RGARPENLML LKEDYPSLKV VMLEQNYRST SRILRCANVL IANNPHDFEK
     QLWSEMGVGD EIRVIRCKNE EAEAERVAME ILTLHLRTDR PYSDFAILYR GNYQAKLIEL
     KLQHHQVPYR LSGGNSFFAR QEVKDLMAYL RLLVNPDDDN AYLRVINVPR REIGSTTLEK
     LGNYATERGV SMYAASEEMG LGEHLDARYT ERLQRFKHWL DGVRHKVALD DPIAALHEMV
     KDIDYENWIR QNTASDKAAD FRIGNVWFLI DALKNTLEKD EEGDMTIEDA IGKLVLRDML
     ERQQEEEENA EGVQMMTLHA SKGLEFPYVF IMGMEEEILP HRSSIEADTI EEERRLAYVG
     ITRARQTLAF TFAAKRKQYG EIIDCTPSRF LDELPPDDLA WEGLDDAPVE VKAARGNNAL
     ADIRAMLKR
//
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