DNAT_ECOLI
ID DNAT_ECOLI Reviewed; 179 AA.
AC P0A8J2; P07904; Q2M5V4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Primosomal protein 1;
DE AltName: Full=Primosomal protein I;
GN Name=dnaT; OrderedLocusNames=b4362, JW4326;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-41.
RX PubMed=3006041; DOI=10.1073/pnas.83.5.1256;
RA Masai H., Bond M.W., Arai K.;
RT "Cloning of the Escherichia coli gene for primosomal protein I: the
RT relationship to dnaT, essential for chromosomal DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1256-1260(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2844800; DOI=10.1016/s0021-9258(18)68149-9;
RA Masai H., Arai K.;
RT "Operon structure of dnaT and dnaC genes essential for normal and stable
RT DNA replication of Escherichia coli chromosome.";
RL J. Biol. Chem. 263:15083-15093(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-179.
RX PubMed=3301836; DOI=10.1016/s0021-9258(18)60985-8;
RA Nakayama N., Bond M.W., Miyajima A., Kobori J., Arai K.;
RT "Structure of Escherichia coli dnaC. Identification of a cysteine residue
RT possibly involved in association with dnaB protein.";
RL J. Biol. Chem. 262:10475-10480(1987).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: This protein is required for primosome-dependent normal DNA
CC replication; it is also involved in inducing stable DNA replication
CC during SOS response. It forms, in concert with DnaB protein and other
CC prepriming proteins DnaC, N, N', N'' a prepriming protein complex on
CC the specific site of the template DNA recognized by protein N'.
CC -!- INTERACTION:
CC P0A8J2; P0A8J2: dnaT; NbExp=2; IntAct=EBI-549621, EBI-549621;
CC P0A8J2; P07013: priB; NbExp=4; IntAct=EBI-549621, EBI-1125223;
CC -!- SIMILARITY: Belongs to the DnaT family. {ECO:0000305}.
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DR EMBL; J04030; AAA23699.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97261.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77318.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78352.1; -; Genomic_DNA.
DR PIR; S56589; RMECI.
DR RefSeq; NP_418782.1; NC_000913.3.
DR RefSeq; WP_000098818.1; NZ_STEB01000025.1.
DR PDB; 2RU8; NMR; -; A=89-179.
DR PDB; 4OU6; X-ray; 1.96 A; A/B/C/D/E=84-159.
DR PDB; 4OU7; X-ray; 2.83 A; A/B/C/D/E=84-154.
DR PDBsum; 2RU8; -.
DR PDBsum; 4OU6; -.
DR PDBsum; 4OU7; -.
DR AlphaFoldDB; P0A8J2; -.
DR SMR; P0A8J2; -.
DR BioGRID; 4262774; 122.
DR ComplexPortal; CPX-1951; Replication restart pre-primosome complex, priAB variant.
DR ComplexPortal; CPX-1952; Replication restart pre-primosome complex, priAC variant.
DR ComplexPortal; CPX-5909; Replication restart primosome complex, priAC variant.
DR ComplexPortal; CPX-5910; Replication restart primosome complex, priAB variant.
DR DIP; DIP-47957N; -.
DR IntAct; P0A8J2; 6.
DR MINT; P0A8J2; -.
DR STRING; 511145.b4362; -.
DR jPOST; P0A8J2; -.
DR PaxDb; P0A8J2; -.
DR PRIDE; P0A8J2; -.
DR EnsemblBacteria; AAC77318; AAC77318; b4362.
DR EnsemblBacteria; BAE78352; BAE78352; BAE78352.
DR GeneID; 66671752; -.
DR GeneID; 948813; -.
DR KEGG; ecj:JW4326; -.
DR KEGG; eco:b4362; -.
DR PATRIC; fig|1411691.4.peg.2324; -.
DR EchoBASE; EB0240; -.
DR eggNOG; ENOG502Z8PW; Bacteria.
DR HOGENOM; CLU_1501592_0_0_6; -.
DR OMA; ASFVAYW; -.
DR PhylomeDB; P0A8J2; -.
DR BioCyc; EcoCyc:EG10244-MON; -.
DR BioCyc; MetaCyc:EG10244-MON; -.
DR PRO; PR:P0A8J2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990158; C:DnaB-DnaC-DnaT-PriA-PriB complex; IDA:EcoCyc.
DR GO; GO:1990159; C:DnaB-DnaC-DnaT-PriA-PriC complex; IC:ComplexPortal.
DR GO; GO:1990077; C:primosome complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IC:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:EcoCyc.
DR GO; GO:0070207; P:protein homotrimerization; IDA:EcoCyc.
DR GO; GO:0031297; P:replication fork processing; IDA:EcoCyc.
DR HAMAP; MF_01061; DnaT; 1.
DR InterPro; IPR020917; DnaT.
DR InterPro; IPR040480; DnaT_DNA_bind.
DR Pfam; PF17948; DnaT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; Primosome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3006041"
FT CHAIN 2..179
FT /note="Primosomal protein 1"
FT /id="PRO_0000199869"
FT REGION 156..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 28
FT /note="E -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4OU6"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:4OU6"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:4OU6"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4OU6"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:4OU6"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:4OU6"
SQ SEQUENCE 179 AA; 19455 MW; 8DE048A3B2A6235B CRC64;
MSSRVLTPDV VGIDALVHDH QTVLAKAEGG VVAVFANNAP AFYAVTPARL AELLALEEKL
ARPGSDVALD DQLYQEPQAA PVAVPMGKFA MYPDWQPDAD FIRLAALWGV ALREPVTTEE
LASFIAYWQA EGKVFHHVQW QQKLARSLQI GRASNGGLPK RDVNTVSEPD SQIPPGFRG
