ID D2UGY2_XANAP Unreviewed; 658 AA.
AC D2UGY2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 ECO:0000313|EMBL:CBA17643.1};
GN OrderedLocusNames=XALc_3164 {ECO:0000313|EMBL:CBA17643.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17643.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA17643.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
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; FP565176; CBA17643.1; -; Genomic_DNA.
DR RefSeq; WP_012917636.1; NC_013722.1.
DR AlphaFoldDB; D2UGY2; -.
DR STRING; 380358.XALC_3164; -.
DR GeneID; 57878481; -.
DR KEGG; xal:XALC_3164; -.
DR PATRIC; fig|29447.3.peg.3145; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000001890; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001890}.
FT DOMAIN 2..278
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 279..552
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 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ SEQUENCE 658 AA; 72965 MW; 1FDE1F94D3C170F1 CRC64;
MHGLNPPQRA AVLHDEGPLL VLAGAGSGKT RVIVEKIAHL IASGRYPAKR IAAITFTNKS
AKEMRERVAK RIRNEAADGL TICTFHALGL KFLQIEHAAV GLKRGFSIFD ADDAAAQIKD
LMPGAKPDAV DDVKNLISRA KNAGLSPEQA MAAARSNREQ DAASLYARYQ ARLSTFNAVD
FDDLIRLPVQ VLESNEDIVM AWRERIGYLL VDESQDTNDA QYRLLKMLAG PRGNFTCVGD
DDQSIYAWRG ANPENLMQMG RDYPTLQIIK LEQNYRCSNR VLRAANALIA HNPHEHLKTL
WSDQADGERI RVWECRDSDH EAEKVAAEIA YLGTAKQVPW SDFCILFRGN FQSRPLEKAL
QMAAVPYHIT GGTAFLERQE VKDVLAWLRL LVNPDDDAAF LRAVQAPKRE VGATSLAKLA
ELAAAKHLPM SRAAASVGAL QQLPPRAANG LSDFVDILHE LRAASATVSS ADVVRQLAEQ
SGLIRELRNQ CKDEASFQRR RGNLEELAKW FESGPRGASV GDLAAQLALL SRNDKDDGGN
QVRMMTMHAS KGLEFRYVFI VGCEDGVLPH EVSLEEGNLQ EERRLLYVGI TRAKEQLWMS
YSMLTRKFGE HIRLKPSRFF DEIPAEEMQR DGADPVADAA RKKERANAGL AAIQALFD
//
