DIAA_ECOLI
ID DIAA_ECOLI Reviewed; 196 AA.
AC P66817; P45466; Q2M961;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DnaA initiator-associating protein DiaA;
GN Name=diaA; Synonyms=yraO; OrderedLocusNames=b3149, JW3118;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-7, FUNCTION, INTERACTION WITH DNAA, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=15326179; DOI=10.1074/jbc.m402762200;
RA Ishida T., Akimitsu N., Kashioka T., Hatano M., Kubota T., Ogata Y.,
RA Sekimizu K., Katayama T.;
RT "DiaA, a novel DnaA-binding protein, ensures the timely initiation of
RT Escherichia coli chromosome replication.";
RL J. Biol. Chem. 279:45546-45555(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, INTERACTION WITH DNAA,
RP SUBUNIT, AND MUTAGENESIS OF SER-52; ARG-71; PRO-72; ASN-83; LYS-101;
RP LEU-190 AND PHE-191.
RX PubMed=17699754; DOI=10.1101/gad.1561207;
RA Keyamura K., Fujikawa N., Ishida T., Ozaki S., Su'etsugu M., Fujimitsu K.,
RA Kagawa W., Yokoyama S., Kurumizaka H., Katayama T.;
RT "The interaction of DiaA and DnaA regulates the replication cycle in E.
RT coli by directly promoting ATP DnaA-specific initiation complexes.";
RL Genes Dev. 21:2083-2099(2007).
CC -!- FUNCTION: Required for the timely initiation of chromosomal replication
CC via direct interactions with the DnaA initiator protein.
CC {ECO:0000269|PubMed:15326179, ECO:0000269|PubMed:17699754}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. May be in a rapid association-
CC dissociation equilibrium between homodimers and homotetramers.
CC Formation of homotetramers is required for stimulation of replication.
CC Interacts with DnaA. {ECO:0000269|PubMed:15326179,
CC ECO:0000269|PubMed:17699754}.
CC -!- INTERACTION:
CC P66817; P66817: diaA; NbExp=5; IntAct=EBI-1125806, EBI-1125806;
CC P66817; P03004: dnaA; NbExp=5; IntAct=EBI-1125806, EBI-548951;
CC -!- SIMILARITY: Belongs to the SIS family. DiaA subfamily. {ECO:0000305}.
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DR EMBL; U18997; AAA57952.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76183.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77195.1; -; Genomic_DNA.
DR PIR; A65105; A65105.
DR RefSeq; NP_417618.1; NC_000913.3.
DR RefSeq; WP_001158034.1; NZ_STEB01000012.1.
DR PDB; 2YVA; X-ray; 1.85 A; A/B=1-196.
DR PDB; 4U6N; X-ray; 1.91 A; A=2-196.
DR PDBsum; 2YVA; -.
DR PDBsum; 4U6N; -.
DR AlphaFoldDB; P66817; -.
DR SMR; P66817; -.
DR BioGRID; 4261991; 149.
DR ComplexPortal; CPX-1963; dnaA-diaA complex.
DR DIP; DIP-35981N; -.
DR IntAct; P66817; 10.
DR STRING; 511145.b3149; -.
DR jPOST; P66817; -.
DR PaxDb; P66817; -.
DR PRIDE; P66817; -.
DR EnsemblBacteria; AAC76183; AAC76183; b3149.
DR EnsemblBacteria; BAE77195; BAE77195; BAE77195.
DR GeneID; 67414914; -.
DR GeneID; 947661; -.
DR KEGG; ecj:JW3118; -.
DR KEGG; eco:b3149; -.
DR PATRIC; fig|1411691.4.peg.3581; -.
DR EchoBASE; EB2633; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_3_1_6; -.
DR InParanoid; P66817; -.
DR OMA; DVHICVP; -.
DR PhylomeDB; P66817; -.
DR BioCyc; EcoCyc:YRAO-MON; -.
DR EvolutionaryTrace; P66817; -.
DR PRO; PR:P66817; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990102; C:DnaA-DiaA complex; IPI:ComplexPortal.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IDA:EcoCyc.
DR CDD; cd05006; SIS_GmhA; 1.
DR HAMAP; MF_01157; SIS_DiaA; 1.
DR InterPro; IPR023070; DiaA.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication;
KW Reference proteome.
FT CHAIN 1..196
FT /note="DnaA initiator-associating protein DiaA"
FT /id="PRO_0000136555"
FT DOMAIN 34..196
FT /note="SIS"
FT REGION 190..191
FT /note="Important for interaction with DnaA"
FT MUTAGEN 52
FT /note="S->F: Abolishes stimulation of DnaA-dependent DNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 71
FT /note="R->Q: Reduces affinity for DnaA. Strongly reduces
FT DnaA-dependent DNA synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 72
FT /note="P->A,S: Strongly reduces affinity for DnaA. Reduces
FT DnaA-dependent DNA synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 83
FT /note="N->D: Abolishes association of homodimers into
FT homotetramers. Reduces affinity for DnaA. Strongly reduces
FT DnaA-dependent DNA synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 101
FT /note="K->E: Abolishes association of homodimers into
FT homotetramers. Strongly reduces DnaA-dependent DNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 190
FT /note="L->A,P: Abolishes interaction with DnaA. Strongly
FT reduces DnaA-dependent DNA synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT MUTAGEN 191
FT /note="F->L,S: Abolishes interaction with DnaA. Strongly
FT reduces DnaA-dependent DNA synthesis."
FT /evidence="ECO:0000269|PubMed:17699754"
FT HELIX 2..22
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2YVA"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2YVA"
FT HELIX 168..190
FT /evidence="ECO:0007829|PDB:2YVA"
SQ SEQUENCE 196 AA; 21106 MW; F9ADFE9C0DF365A8 CRC64;
MQERIKACFT ESIQTQIAAA EALPDAISRA AMTLVQSLLN GNKILCCGNG TSAANAQHFA
ASMINRFETE RPSLPAIALN TDNVVLTAIA NDRLHDEVYA KQVRALGHAG DVLLAISTRG
NSRDIVKAVE AAVTRDMTIV ALTGYDGGEL AGLLGPQDVE IRIPSHRSAR IQEMHMLTVN
CLCDLIDNTL FPHQDD
