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Entry: A0A1G5A456_9BURK
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ID   A0A1G5A456_9BURK        Unreviewed;       699 AA.
AC   A0A1G5A456;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SAMN03159363_4383 {ECO:0000313|EMBL:SCX72659.1};
OS   Variovorax sp. EL159.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX72659.1, ECO:0000313|Proteomes:UP000199507};
RN   [1] {ECO:0000313|EMBL:SCX72659.1, ECO:0000313|Proteomes:UP000199507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL159 {ECO:0000313|EMBL:SCX72659.1,
RC   ECO:0000313|Proteomes:UP000199507};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMUJ01000005; SCX72659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5A456; -.
DR   STRING; 1566270.SAMN03159363_4383; -.
DR   OrthoDB; 5905204at2; -.
DR   Proteomes; UP000199507; 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   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}.
FT   DOMAIN          3..277
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          278..578
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         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ   SEQUENCE   699 AA;  78076 MW;  A89899FE132A7D1B CRC64;
     MSHGLNLAQQ EAVNYMHGPC LVLAGAGSGK TRVITHKIGR LIQSGLDPKR IAAITFTNKA
     AAEMRERAKD LIGKDARKVV VCTFHALGVR MMREDGAVLG LKPAFSILDS DDVTKILKDA
     GGTTDIATAR IWQWTISKWK NMGLNAEQAA AIAVDDNERI TAEVMGHYQE RLQAYQSVDF
     DDLIGMPLKL LHDFPEVRAK WQAALGHILV DEYQDTNATQ YEVLKALAGE RGRFTAVGDD
     DQSIYGWRGA TLDNLRKLPV DYPTLKVIKL EQNYRSTSAI LRAANNVIGP NPKLFPKTLF
     SELGEGEPVR IVDADSELHE AERAVARIVS LRAGDATTQG KQYKEFRDFA ILYRANHQAR
     VFEQALRKAQ IPYKVSGGQS FFDRAEIKDL CGWFRLWVNN DDDPAFLRAI TTPKRGIGHT
     TLASLGTFAS QYKLSLFAAL FSPSLPSVIP KRTLEGVYEF GRYINDLEYR ARRTMGAEDS
     RAFMLEWLKE IDYEQHLYEG EDSEAAAASR WNNVMEFVDW MSQRAGGSLD DASGANDNET
     ERKSLLEVAQ TISLLSTISE REQDQDVVTL STLHASKGLE WPHVILIGVT EGLLPFKLDD
     DNGRQKMVSD DTLQRLQEER RLMYVGITRA QRSLAVSWTK KRKQGRDMVP CVPSRFIAEM
     GLDKETTKED PREKLKALRA EFARKAQDSA AAKAAAAAS
//
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