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Database: UniProt
Entry: A0A0G9HFY4_9GAMM
LinkDB: A0A0G9HFY4_9GAMM
Original site: A0A0G9HFY4_9GAMM 
ID   A0A0G9HFY4_9GAMM        Unreviewed;       664 AA.
AC   A0A0G9HFY4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=BJI69_05475 {ECO:0000313|EMBL:APG03420.1};
OS   Luteibacter rhizovicinus DSM 16549.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG03420.1, ECO:0000313|Proteomes:UP000182987};
RN   [1] {ECO:0000313|Proteomes:UP000182987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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; CP017480; APG03420.1; -; Genomic_DNA.
DR   RefSeq; WP_046966525.1; NZ_JPLB01000015.1.
DR   AlphaFoldDB; A0A0G9HFY4; -.
DR   STRING; 1440763.BJI69_05475; -.
DR   KEGG; lrz:BJI69_05475; -.
DR   PATRIC; fig|1440763.5.peg.556; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000182987; 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|HAMAP-Rule:MF_01920, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01920}.
FT   DOMAIN          1..277
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          278..555
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         21..28
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   664 AA;  74092 MW;  B088B70585BCE817 CRC64;
     MLNPQQHAAV EYCDGPLLVL AGAGSGKTRV ITEKISHLIS HRHLAAEKIA AITFTNKAAK
     EMRERVGRLI SEQSAKALTV CTFHALGLKF LQIEHDRAQL RRGFSVLDAD DSANMIKELS
     PKGVKPEVIQ GIRNLVGKAK NGGLTPEEAM AAARSPREIE AATIYDLYQQ RLAAFNAVDF
     DDLIRLPLRI LESDDDARAI WQERLRYLLV DEYQDTNDAQ YRLLKAIAGP KARFTCVGDD
     DQSIYAWRGA NPENIDQLGR DFTNLRVIKL EQNYRCAKRI LRAANQLIAN NPHVHDKKLW
     SDHVEGPPIR VLECKDNDHE AERIAAIASS LHEKYKEKGA RWDDFCILYR GNFQARVLEK
     ALRLAKVPYH LSGALSFLDR AEVKDILCYL RLLTNPTDDA AFLRVVNVPK REIGSTSLEK
     LGQMAQTRNA SLLEATRSDA VLKTISSRPA SALAGFSRLM DELRSDANHL SAADLVQTII
     EKTGYGAQIA ASTPDDVLRE RRLGNLRELA DWFRAMSKDG GRTGDIAAQL ALLSHADRDD
     PGNALRMMTL HSAKGLEFRF VFIVGCEDGT LPHEGAIDEG RLDEERRLMY VGITRAKEML
     TLSFSARSRK YGEVLSNDPS RFLEELPQDD LHWDGKDPEA DAEVKMETAA THMARIRAML
     AGGA
//
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