ID Q6CZH2_PECAS Unreviewed; 720 AA.
AC Q6CZH2;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
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:CAG77076.1};
GN Synonyms=mutU {ECO:0000313|EMBL:CAG77076.1}, pdeB
GN {ECO:0000313|EMBL:CAG77076.1}, rad {ECO:0000313|EMBL:CAG77076.1}, recL
GN {ECO:0000313|EMBL:CAG77076.1};
GN OrderedLocusNames=ECA4179 {ECO:0000313|EMBL:CAG77076.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG77076.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG77076.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG77076.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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; BX950851; CAG77076.1; -; Genomic_DNA.
DR RefSeq; WP_011095650.1; NC_004547.2.
DR AlphaFoldDB; Q6CZH2; -.
DR STRING; 218491.ECA4179; -.
DR GeneID; 57210841; -.
DR KEGG; eca:ECA4179; -.
DR PATRIC; fig|218491.5.peg.4252; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_5_6; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000007966; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007966}.
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; 81814 MW; EE3B35F362E0EC4A CRC64;
MDVSDLLDGL NDKQRAAVAA PRSNLLVLAG AGSGKTRVLV HRIAWLLSVE NCSPYSIMAV
TFTNKAAAEM RHRINHLIGT SQGGMWIGTF HGLAHRLLRA HHMDANLPQD FQILDSDDQL
RLLKRLIRAL NLDEKQWPPR QAMWFINGKK DEGLRPQHIE SYGNPIEQTW QRVYQAYQEA
CDRAGLVDFA ELLLRAHELW LNKPHVLNHY RERFTNILVD EFQDTNRIQY AWIHMLAGDS
AKVMIVGDDD QSIYGWRGAQ VENIQLFLKD FAGAETIRLE QNYRSTSNIL KAANALIAHN
GGRLGKNLWT EGVEGEPISL YCAFNELDEA RYVVNRIKAW QEKGGVLKDN AILYRSNAQS
RVLEEALLQQ SMPYRIYGGM RFFERQEIRD SLSYLRLISN RNDDAAFERV VNTPTRGIGD
RTLDVVRQTA RDRQLTLWQS TRVLLQEKVL AGRAAASLQR FVELIDALAY ETSELPLHVQ
TDRAIKDSGL WSMYEQEKGE KGQARVENLE ELVTATRQFS YQEEDQDLMP LQAFLSHAAL
EAGEGQADAN QDAVQLMTLH SAKGLEFPQV FIVGMEEGMF PSQMSLDEGG RLEEERRLAY
VGVTRAMEKL TITYAESRRL YGKEAYHRPS RFVGELPEEC VEEVRLRASV SRPVNHQRLG
TPITENDSGY KLGQRVRHAK FGEGTIVNLE GSGEHARLQV AFQGQGIKWL VAAYARLETV
//
