ID D2TSV7_CITRI Unreviewed; 604 AA.
AC D2TSV7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN OrderedLocusNames=ROD_50011 {ECO:0000313|EMBL:CBG91675.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91675.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91675.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91675.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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};
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DR EMBL; FN543502; CBG91675.1; -; Genomic_DNA.
DR AlphaFoldDB; D2TSV7; -.
DR STRING; 637910.ROD_50011; -.
DR KEGG; cro:ROD_50011; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_028798_0_0_6; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR011528; NERD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF08378; NERD; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CBG91675.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 26..115
FT /note="NERD"
FT /evidence="ECO:0000259|Pfam:PF08378"
FT DOMAIN 416..520
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13361"
FT DOMAIN 537..588
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
SQ SEQUENCE 604 AA; 68663 MW; F8A5D367619A8000 CRC64;
MILLEHEYVM AKLINVSAST EERMTPGERR VASRLESFLN DDCLVWYDIP VGRKNRHPDF
VIIDPDNGLV FLEVKDWTVS TLRKANQEQV TLETDGLLKS EINPLVQVRR YACDTVNALP
ADPCLRQNDG QYKGRLNLAW AYGVVFTRIT RQQLKALTGN DENAVEKIFP SAQTICQDEM
TQSVLPEVFR QKIAGMFTTG FRTRVTPRMR DILRAHLFPE VTVKQNSQIK IMDIQQEILA
RNIGDGHRVI HGVAGSGKTM ILLCRCLYLA ETTSGKILVL CYNITLASYL RECIEARGLR
SRVTVSHFHS WCASMAKRHG IQVTADRKEY PEKCFSTLEE AVNSGKITQT GYDAVLVDEG
HDFDSRWLAL IARLFDNASR SLLLMYDDAQ SIYRRERALN FSLASVGIQA QGRTSVLPVN
YRNPKRILHF AYAFSREYFE KHQNREIPLV QPQAGGEEGT EPEILRCASE RDEARQVADW
LEKRHALCGH WSDMAVLCPA EFSVKQLKEV MTQRGIPFAT CFDSEGKKAY SRRKDVVHLL
TYQSSKGLEF PYVAVINASF VPSGVADESE VIPVLYVAFT RATRELLVTC YRENSISRHL
EDFA
//
