ID UVSW_BPT4 Reviewed; 587 AA.
AC P20703;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=ATP-dependent DNA helicase uvsW;
DE EC=3.6.4.12;
DE AltName: Full=Dar protein;
GN Name=uvsW; Synonyms=dar;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS, AND CHARACTERIZATION.
RX PubMed=9233823; DOI=10.1093/emboj/16.13.4142;
RA Carles-Kinch K., George J.W., Kreuzer K.N.;
RT "Bacteriophage T4 UvsW protein is a helicase involved in recombination,
RT repair and the regulation of DNA replication origins.";
RL EMBO J. 16:4142-4151(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
RX PubMed=2377482; DOI=10.1093/nar/18.14.4277;
RA Kaliman A.V., Khasanova M.A., Kryukov V.M., Tanyashin V.I., Bayev A.A.;
RT "The nucleotide sequence of the region of bacteriophage T4 inh(lip)-hoc
RT genes.";
RL Nucleic Acids Res. 18:4277-4277(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=2388264; DOI=10.1016/0022-2836(90)90283-r;
RA Derr L.K., Kreuzer K.N.;
RT "Expression and function of the uvsW gene of bacteriophage T4.";
RL J. Mol. Biol. 214:643-656(1990).
RN [5]
RP FUNCTION.
RX PubMed=24013402; DOI=10.1038/ncomms3368;
RA Manosas M., Perumal S.K., Bianco P., Ritort F., Benkovic S.J.,
RA Croquette V.;
RT "RecG and UvsW catalyse robust DNA rewinding critical for stalled DNA
RT replication fork rescue.";
RL Nat. Commun. 4:2368-2368(2013).
RN [6]
RP FUNCTION, AND INTERACTION WITH GP32.
RX PubMed=23732982; DOI=10.1016/j.jmb.2013.05.012;
RA Perumal S.K., Nelson S.W., Benkovic S.J.;
RT "Interaction of T4 UvsW helicase and single-stranded DNA binding protein
RT gp32 through its carboxy-terminal acidic tail.";
RL J. Mol. Biol. 425:2823-2839(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-282.
RX PubMed=15062081; DOI=10.1016/j.str.2004.02.016;
RA Sickmier E.A., Kreuzer K.N., White S.W.;
RT "The crystal structure of the UvsW helicase from bacteriophage T4.";
RL Structure 12:583-592(2004).
CC -!- FUNCTION: Plays important roles in recombination-dependent DNA repair
CC and the reorganization of stalled replication forks during viral DNA
CC synthesis. {ECO:0000269|PubMed:23732982, ECO:0000269|PubMed:24013402}.
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=3.6.4.12;
CC -!- SUBUNIT: Interacts with gp32. {ECO:0000269|PubMed:23732982}.
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DR EMBL; AF158101; AAD42668.1; -; Genomic_DNA.
DR EMBL; X56097; CAA39576.1; -; Genomic_DNA.
DR EMBL; X14869; CAA33014.1; -; Genomic_DNA.
DR PIR; PQ0097; S10498.
DR RefSeq; NP_049796.1; NC_000866.4.
DR PDB; 1RIF; X-ray; 2.00 A; A/B=1-282.
DR PDB; 2JPN; NMR; -; A=512-587.
DR PDB; 2OCA; X-ray; 2.70 A; A=1-502.
DR PDBsum; 1RIF; -.
DR PDBsum; 2JPN; -.
DR PDBsum; 2OCA; -.
DR BMRB; P20703; -.
DR SMR; P20703; -.
DR GeneID; 1258733; -.
DR KEGG; vg:1258733; -.
DR OrthoDB; 2008at10239; -.
DR EvolutionaryTrace; P20703; -.
DR Proteomes; UP000009087; Segment.
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:0004386; F:helicase activity; IDA:CACAO.
DR CDD; cd18031; DEXHc_UvsW; 1.
DR Gene3D; 1.20.1280.210; -; 1.
DR Gene3D; 3.30.780.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020975; UvsW.1_dom.
DR InterPro; IPR049409; UvsW_N.
DR InterPro; IPR049430; UvsW_N_sf.
DR InterPro; IPR038341; UvsW_sf.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF11637; UvsW-1; 1.
DR Pfam; PF21241; UvsW_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Late protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..587
FT /note="ATP-dependent DNA helicase uvsW"
FT /id="PRO_0000164988"
FT DOMAIN 122..280
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 335..501
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 141
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9233823"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1RIF"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1RIF"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1RIF"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1RIF"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1RIF"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1RIF"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:2OCA"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:2OCA"
FT HELIX 476..490
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:2OCA"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:2JPN"
FT HELIX 518..523
FT /evidence="ECO:0007829|PDB:2JPN"
FT HELIX 528..533
FT /evidence="ECO:0007829|PDB:2JPN"
FT HELIX 538..551
FT /evidence="ECO:0007829|PDB:2JPN"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:2JPN"
FT HELIX 560..578
FT /evidence="ECO:0007829|PDB:2JPN"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:2JPN"
SQ SEQUENCE 587 AA; 67525 MW; D7FBD8CE1E38C7CA CRC64;
MDIKVHFHDF SHVRIDCEES TFHELRDFFS FEADGYRFNP RFRYGNWDGR IRLLDYNRLL
PFGLVGQIKK FCDNFGYKAW IDPQINEKEE LSRKDFDEWL SKLEIYSGNK RIEPHWYQKD
AVFEGLVNRR RILNLPTSAG KSLIQALLAR YYLENYEGKI LIIVPTTALT TQMADDFVDY
RLFSHAMIKK IGGGASKDDK YKNDAPVVVG TWQTVVKQPK EWFSQFGMMM NDECHLATGK
SISSIISGLN NCMFKFGLSG SLRDGKANIM QYVGMFGEIF KPVTTSKLME DGQVTELKIN
SIFLRYPDEF TTKLKGKTYQ EEIKIITGLS KRNKWIAKLA IKLAQKDENA FVMFKHVSHG
KAIFDLIKNE YDKVYYVSGE VDTETRNIMK TLAENGKGII IVASYGVFST GISVKNLHHV
VLAHGVKSKI IVLQTIGRVL RKHGSKTIAT VWDLIDSAGV KPKSANTKKK YVHLNYLLKH
GIDRIQRYAD EKFNYVMKTV NLISFGPLEK KMLLEFKQFL YEASIDEFMG KIASCQTLEG
LEELEAYYKK RVKETELKDT DDISVRDALA GKRAELEDSD DEVEESF
//
