ID A0A240U6Q7_9BURK Unreviewed; 693 AA.
AC A0A240U6Q7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=CBP34_17260 {ECO:0000313|EMBL:ART53060.1};
OS Acidovorax carolinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART53060.1, ECO:0000313|Proteomes:UP000194432};
RN [1] {ECO:0000313|EMBL:ART53060.1, ECO:0000313|Proteomes:UP000194432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA3 {ECO:0000313|EMBL:ART53060.1};
RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA Aitken M.D.;
RT "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL Submitted (MAY-2017) 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; CP021361; ART53060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240U6Q7; -.
DR KEGG; acin:CBP34_17260; -.
DR Proteomes; UP000194432; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000194432}.
FT DOMAIN 3..278
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 279..573
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ SEQUENCE 693 AA; 76631 MW; ADBB20A0F66EB41E CRC64;
MSAGLNLAQL QAVHYTDGAC LVLAGAGSGK TRVITHKIAH MIERGMEPKR IAAITFTNKA
AAEMRERAKG LIGRRAKDVL VCTFHALGVR MVREDGAVLG LKPQFSIMDA DDVAGILKDA
AGGTTDLATA RQWQWTISKW KNMGLTSGQA LAQATDDNER SIAVVMARYE ERLAAYQSVD
FDDLIGMPLK LLRDFPEVRA KWQAALAHVL VDEYQDTNAT QYELLKLLVG ERGHFTAVGD
DDQSIYGWRG ATLDNLKKLP LDYPALKVIK LEQNYRSTSA ILRAANNVIG PNPKLFPKTL
FSELGEGDPV RVVDADTEEH EADRAVARIQ SLRAAANPPP AWKDFAILYR ANHQAKPFEK
ALRRANIPYK VSGGTSFFDR AEIKDLCAWF RLWINNDDDP AFLRAIGSPK RGIGHTTLAA
LGAFATQHKQ SMFGALFNGM LPAAVPKRAL DGLHEFGRYI NDLEHRARHT HGAEASRAFL
ADWLKEIGYE QHLYDGEDSE KVAAARWTNV LEFCDWMAQR AGGQIDDTAG AVVAKETKSL
LEVSQTIALL STISEREQEQ DMVTLSTLHA SKGLEWPHVI LVGVTEGMLP FKLDDDEGRQ
LKVADDTLQR LQEERRLMYV GITRAQRTLA VSWTKKRKKG REMVAARPSR FIAEMGLDKA
TTREDPREKL KALRAEFAAK AQAASAANAA PTA
//
