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Database: UniProt
Entry: A0A1V4LMC8_9PSED
LinkDB: A0A1V4LMC8_9PSED
Original site: A0A1V4LMC8_9PSED 
ID   A0A1V4LMC8_9PSED        Unreviewed;       669 AA.
AC   A0A1V4LMC8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=BZ163_21375 {ECO:0000313|EMBL:OPK08429.1};
OS   Pseudomonas sp. VI4.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK08429.1, ECO:0000313|Proteomes:UP000189889};
RN   [1] {ECO:0000313|EMBL:OPK08429.1, ECO:0000313|Proteomes:UP000189889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VI4.1 {ECO:0000313|EMBL:OPK08429.1,
RC   ECO:0000313|Proteomes:UP000189889};
RA   Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA   Gawronski S., Vangronsveld J.;
RT   "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT   isolate from crude oil contaminated soil in Bobrka, Poland.";
RL   Submitted (FEB-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}.
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:OPK08429.1}.
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DR   EMBL; MULM01000169; OPK08429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4LMC8; -.
DR   Proteomes; UP000189889; Unassembled WGS sequence.
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;  76450 MW;  E5E30357BBE4DE95 CRC64;
     MSRLNPRQQE AVSYVGGPLL VLAGAGSGKT SVITRKIAHL VQNCGIRAQY IVAMTFTNKA
     AREMKERVGT LLKGGEGRGL TVCTFHNLGL NIIRKEHVRL GYKPGFSIFD ETDVKALMTD
     IMQKEYSGDD GVDEIKNMIG SWKNDLILPP EALENARNPK EQTAAIVYTH YQRTLKAFNA
     VDFDDLILLP VKLFQEHADI LEKWQNKVRY LLVDEYQDTN ASQYLLVKLL IGTRNQFTVV
     GDDDQSIYAW RGARPENLML LKDDYPSLKV VMLEQNYRST SRILRCANVL ISNNPHEFEK
     QLWSEMGHGD EIRVIRCRNE DAEAERVAVE ILSLHLRTDR PYSDFAILYR GNYQAKLIEL
     KLQHHQVPYR LSGGNSFFGR QEVKDLMAYF RLIVNPDDDN AFLRVINVPR REIGSTTLEK
     LGNYATERKI SMYAATDEIG LGEHLDARFT DRLSRFKRFM DKVREQCAGE DPISALRSMV
     MDIDYENWLR TNSSSDKAAD YRMGNVWFLI EALKNTLEKD EEGEMTVEDA IGKLVLRDML
     ERQQEEEDGA EGVQMMTLHA SKGLEFPYVF IMGMEEEILP HRSSIEADTI EEERRLAYVG
     ITRARQTLAF TFAAKRKQYG EIIDCAPSRF LDELPPDDLA WEGTDDTPVE VKAVRGNTAL
     ADIRAMLKR
//
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