GenomeNet

Database: UniProt
Entry: D2TV17_CITRI
LinkDB: D2TV17_CITRI
Original site: D2TV17_CITRI 
ID   D2TV17_CITRI            Unreviewed;       720 AA.
AC   D2TV17;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
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   Name=uvrD {ECO:0000313|EMBL:CBG90641.1};
GN   OrderedLocusNames=ROD_39381 {ECO:0000313|EMBL:CBG90641.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG90641.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG90641.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG90641.1,
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};
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|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN543502; CBG90641.1; -; Genomic_DNA.
DR   RefSeq; WP_012907916.1; NC_013716.1.
DR   AlphaFoldDB; D2TV17; -.
DR   STRING; 637910.ROD_39381; -.
DR   KEGG; cro:ROD_39381; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_5_6; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
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   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR01075; uvrD; 1.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 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|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          8..286
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          287..564
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   720 AA;  82007 MW;  D6F21B0BD58D559B CRC64;
     MDVSYLLDSL NDKQREAVAA PRSNMLVLAG AGSGKTRVLV HRIAWLLTVE NNSPYSIMAV
     TFTNKAAAEM RHRIGQLMGT SQGGMWVGTF HGLAHRLLRA HHMDANLPQD FQILDSEDQL
     RLLKRLMKAM NLDDKQWPPR QAMWYINGQK DEGLRPHHLQ SFGNPVEQTW QKVYQAYQEA
     CDRAGLVDFA ELLLRAHELW LNKPHILQHY RERFTNILVD EFQDTNNIQY AWVRLLAGDT
     GKVMIVGDDD QSIYGWRGAQ VENIQRFLND FPGAQTIRLE QNYRSTSNIL SAANALIENN
     NGRLGKKLWT DGVDGEPISL YCAFNELDEA RFVVNRIKTW QDNGGALEQC AILYRSNAQS
     RVLEEALLQA SMPYRIYGGM RFFERQEIKD ALSYLRLIAN RNDDAAFERV VNTPTRGIGD
     RTLDVVRQTS RDRQLTLWQA CRELLQEKAL AGRAASALQR FMELIDALAQ ETADMPLHVQ
     TDRVIRDSGL RTMYEQEKGE KGQTRIENLE ELVTATRQFS YNEEDEDLMP LQAFLSHAAL
     EAGEGQADTW QDAVQLMTLH SAKGLEFPQV FIVGMEEGMF PSQMSLDEGG RLEEERRLAY
     VGVTRAMQKL TLTYAETRRL YGKEVYHRPS RFIGELPEEC VEEVRLRATV SRPVSHQRMG
     TPIAENDTGY KLGQRVRHAK FGEGTIVNLE GSGEHSRLQV AFQGQGIKWL VAAYAKLETV
//
DBGET integrated database retrieval system