DDA_BPT4
ID DDA_BPT4 Reviewed; 439 AA.
AC P32270; Q9T0W1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent DNA helicase dda;
DE EC=3.6.4.12;
GN Name=dda; Synonyms=sud;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, AND
RP INTERACTION WITH UVSX.
RX PubMed=1328208; DOI=10.1016/s0021-9258(19)36738-9;
RA Hacker K.J., Alberts B.M.;
RT "Overexpression, purification, sequence analysis, and characterization of
RT the T4 bacteriophage dda DNA helicase.";
RL J. Biol. Chem. 267:20674-20681(1992).
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 FUNCTION.
RX PubMed=12411580; DOI=10.1073/pnas.232401899;
RA Nanduri B., Byrd A.K., Eoff R.L., Tackett A.J., Raney K.D.;
RT "Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a
RT monomeric molecular motor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14722-14727(2002).
RN [4]
RP FUNCTION IN DNA REPLICATION INITIATION.
RX PubMed=18314134; DOI=10.1016/j.jmb.2008.02.002;
RA Brister J.R.;
RT "Origin activation requires both replicative and accessory helicases during
RT T4 infection.";
RL J. Mol. Biol. 377:1304-1313(2008).
RN [5]
RP FUNCTION.
RX PubMed=22504228; DOI=10.1016/j.jmb.2012.04.007;
RA Byrd A.K., Matlock D.L., Bagchi D., Aarattuthodiyil S., Harrison D.,
RA Croquette V., Raney K.D.;
RT "Dda helicase tightly couples translocation on single-stranded DNA to
RT unwinding of duplex DNA: Dda is an optimally active helicase.";
RL J. Mol. Biol. 420:141-154(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=22658750; DOI=10.1016/j.str.2012.04.013;
RA He X., Byrd A.K., Yun M.K., Pemble C.W., Harrison D., Yeruva L., Dahl C.,
RA Kreuzer K.N., Raney K.D., White S.W.;
RT "The T4 phage SF1B helicase Dda is structurally optimized to perform DNA
RT strand separation.";
RL Structure 20:1189-1200(2012).
CC -!- FUNCTION: DNA helicase that stimulates viral DNA replication and
CC recombination. Plays a role in T4 DNA replication initiation by
CC selecting and activating DNA origins. Acts by dissociating and
CC reassociating with the DNA molecule being unwound. Unwinds DNA as a
CC monomer in a 5'-to-3' direction at a rate of 250 bp/s and can
CC efficiently displace proteins from the DNA.
CC {ECO:0000269|PubMed:12411580, ECO:0000269|PubMed:18314134,
CC ECO:0000269|PubMed:22504228}.
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 UvsX and gene 32 protein.
CC {ECO:0000269|PubMed:1328208}.
CC -!- SIMILARITY: To E.coli recD (exonuclease V). {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Dda (DNA-dependent ATPase) entry;
CC URL="https://en.wikipedia.org/wiki/Dda_%28DNA-dependent_ATPase%29";
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; M93048; AAA32488.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42555.1; -; Genomic_DNA.
DR PIR; A45068; A45068.
DR RefSeq; NP_049632.1; NC_000866.4.
DR PDB; 3UPU; X-ray; 3.30 A; A/B/C=1-439.
DR PDBsum; 3UPU; -.
DR SMR; P32270; -.
DR GeneID; 1258784; -.
DR KEGG; vg:1258784; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004386; F:helicase activity; IDA:CACAO.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041214; SH3_14.
DR Pfam; PF18343; SH3_14; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA replication;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..439
FT /note="ATP-dependent DNA helicase dda"
FT /id="PRO_0000164925"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 54
FT /note="G -> E (in Ref. 1; AAA32488)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="E -> D (in Ref. 1; AAA32488)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="N -> I (in Ref. 1; AAA32488)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> G (in Ref. 1; AAA32488)"
FT /evidence="ECO:0000305"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 296..309
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 318..329
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:3UPU"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:3UPU"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:3UPU"
SQ SEQUENCE 439 AA; 49897 MW; 2CDAC6AB99A5A583 CRC64;
MTFDDLTEGQ KNAFNIVMKA IKEKKHHVTI NGPAGTGKTT LTKFIIEALI STGGTGIILA
APTHAAKKIL SKLSGKEAST IHSILKINPV TYEENVLFEQ KEVPDLAKCR VLICDEVSMY
DRKLFKILLS TIPPWCTIIG IGDNKQIRPV EPGENTAYIS PFFTHKDFYQ CELTEVKRSN
APIIDVATDV RNGKWNYDKV VDGHGVRGFT GDTALRDFMV NYFSIVKSLD DLFENRVMAF
TNKSVDKLNS IIRKKIFETD KDFIVGEIIV MQEPLFKTYK IDGKPVSEII FNNGQLVRII
EAEYTSTFVK ARGVPGEYLI RHWDLTVETY GDDEYYREKI KIISSDEELY KFNLFLAKTA
ETYKNWNKGG KAPWSDFWDA KSQFSKVKAL PASTFHKAQG MSVDRAFIYT PCIHYADVEL
AQQLLYVGVT RGRYDVFYV
