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Entry version 190 (07 Apr 2021)
Sequence version 2 (01 Jul 1993)
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Protein

Chromosomal replication initiator protein DnaA

Gene

dnaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC.
Also required for replication of plasmid DNA; binds 4 dnaA boxes in the minimal plasmid RK2 replication origin (oriV).

Miscellaneous

At least 4 systems specifically target DnaA to prevent more than 1 round of replication initiation per cell cycle. 1: SeqA binds to and sequesters hemimethylated oriC, preventing DnaA binding. 2: ATP-DnaA binds to the chromosomal datA locus, sequestering ATP-DnaA. 3: ATP-DnaA binds to its own promoter, repressing transcription. 4: RIDA (regulatory inactivation of DnaA) via Hda and the DNA-loaded beta clamp hydrolyzes ATP-DnaA to ADP-DnaA.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Acetylation decreases the binding abilities to ATP and ADP and leads to inhibition of DNA replication initiation.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi172 – 179ATPCurated8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA replication inhibitor, DNA-binding, Repressor
Biological processDNA replication, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:PD03831

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Chromosomal replication initiator protein DnaA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:dnaA
Ordered Locus Names:b3702, JW3679
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi178K → Q or R: Loses the ability to bind to ATP or ADP. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001141741 – 467Chromosomal replication initiator protein DnaAAdd BLAST467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei178N6-acetyllysine; by PatZ1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated at Lys-178 by PatZ. Deacetylated by CobB. Is also acetylated nonenzymatically by acetyl-phosphate. Acetylation level increases in a growth phase-dependent manner and peaks at the stationnary phase.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P03004

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P03004

PRoteomics IDEntifications database

More...
PRIDEi
P03004

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P03004

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Some 20 DnaA protein molecules bind their sites in oriC. Forms the RIDA (regulatory inactivation of DnaA) complex with ATP-DnaA, ADP-Hda and the DNA-loaded sliding beta clamp (dnaN).

Interacts with DiaA; this stimulates the association of DnaA with the origin of replication.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261539, 155 interactors
852519, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1943, dnaA oligomeric complex
CPX-1944, DnaA-L2 DNA replication initiation inhibitory complex
CPX-1945, Regulatory inactivation of dnaA (RIDA) complex
CPX-1948, dnaA-dps DNA replication initiation inhibitory complex
CPX-1950, dnaA-dnaB-dnaC loader complex
CPX-1961, DnaA-HU complex, variant hupAB
CPX-1962, DnaA-HU complex, variant hupA
CPX-1963, dnaA-diaA complex

Database of interacting proteins

More...
DIPi
DIP-9455N

Protein interaction database and analysis system

More...
IntActi
P03004, 45 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3702

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P03004

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03004

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DnaA family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0593, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_026910_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P03004

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P03004

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06571, Bac_DnaA_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1750.10, 1 hit
3.30.300.180, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00377, DnaA_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR001957, Chromosome_initiator_DnaA
IPR020591, Chromosome_initiator_DnaA-like
IPR018312, Chromosome_initiator_DnaA_CS
IPR013317, DnaA
IPR013159, DnaA_C
IPR024633, DnaA_N_dom
IPR038454, DnaA_N_sf
IPR027417, P-loop_NTPase
IPR010921, Trp_repressor/repl_initiator

The PANTHER Classification System

More...
PANTHERi
PTHR30050:SF2, PTHR30050:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00308, Bac_DnaA, 1 hit
PF08299, Bac_DnaA_C, 1 hit
PF11638, DnaA_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00051, DNAA

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 1 hit
SM00760, Bac_DnaA_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48295, SSF48295, 1 hit
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00362, DnaA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01008, DNAA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P03004-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW
60 70 80 90 100
VRDKYLNNIN GLLTSFCGAD APQLRFEVGT KPVTQTPQAA VTSNVAAPAQ
110 120 130 140 150
VAQTQPQRAA PSTRSGWDNV PAPAEPTYRS NVNVKHTFDN FVEGKSNQLA
160 170 180 190 200
RAAARQVADN PGGAYNPLFL YGGTGLGKTH LLHAVGNGIM ARKPNAKVVY
210 220 230 240 250
MHSERFVQDM VKALQNNAIE EFKRYYRSVD ALLIDDIQFF ANKERSQEEF
260 270 280 290 300
FHTFNALLEG NQQIILTSDR YPKEINGVED RLKSRFGWGL TVAIEPPELE
310 320 330 340 350
TRVAILMKKA DENDIRLPGE VAFFIAKRLR SNVRELEGAL NRVIANANFT
360 370 380 390 400
GRAITIDFVR EALRDLLALQ EKLVTIDNIQ KTVAEYYKIK VADLLSKRRS
410 420 430 440 450
RSVARPRQMA MALAKELTNH SLPEIGDAFG GRDHTTVLHA CRKIEQLREE
460
SHDIKEDFSN LIRTLSS
Length:467
Mass (Da):52,551
Last modified:July 1, 1993 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i607C8366A8CDCCED
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA62053 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti69 – 70AD → RI (PubMed:6296774).Curated2
Sequence conflicti403 – 407VARPR → GXGPG in AAA62053 (PubMed:7686882).Curated5

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J01602 Genomic DNA Translation: AAB59149.1
X01861 Genomic DNA Translation: CAA25980.1
L10328 Genomic DNA Translation: AAA62053.1 Different initiation.
U00096 Genomic DNA Translation: AAC76725.1
AP009048 Genomic DNA Translation: BAE77592.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65172, IQECDA

NCBI Reference Sequences

More...
RefSeqi
NP_418157.1, NC_000913.3
WP_000059111.1, NZ_STEB01000015.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76725; AAC76725; b3702
BAE77592; BAE77592; BAE77592

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58463270
948217

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3679
eco:b3702

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3826

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01602 Genomic DNA Translation: AAB59149.1
X01861 Genomic DNA Translation: CAA25980.1
L10328 Genomic DNA Translation: AAA62053.1 Different initiation.
U00096 Genomic DNA Translation: AAC76725.1
AP009048 Genomic DNA Translation: BAE77592.1
PIRiG65172, IQECDA
RefSeqiNP_418157.1, NC_000913.3
WP_000059111.1, NZ_STEB01000015.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J1VX-ray2.10A374-467[»]
2E0GNMR-A2-108[»]
SMRiP03004
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261539, 155 interactors
852519, 2 interactors
ComplexPortaliCPX-1943, dnaA oligomeric complex
CPX-1944, DnaA-L2 DNA replication initiation inhibitory complex
CPX-1945, Regulatory inactivation of dnaA (RIDA) complex
CPX-1948, dnaA-dps DNA replication initiation inhibitory complex
CPX-1950, dnaA-dnaB-dnaC loader complex
CPX-1961, DnaA-HU complex, variant hupAB
CPX-1962, DnaA-HU complex, variant hupA
CPX-1963, dnaA-diaA complex
DIPiDIP-9455N
IntActiP03004, 45 interactors
STRINGi511145.b3702

PTM databases

iPTMnetiP03004

Proteomic databases

jPOSTiP03004
PaxDbiP03004
PRIDEiP03004

Genome annotation databases

EnsemblBacteriaiAAC76725; AAC76725; b3702
BAE77592; BAE77592; BAE77592
GeneIDi58463270
948217
KEGGiecj:JW3679
eco:b3702
PATRICifig|511145.12.peg.3826

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0231

Phylogenomic databases

eggNOGiCOG0593, Bacteria
HOGENOMiCLU_026910_0_1_6
InParanoidiP03004
PhylomeDBiP03004

Enzyme and pathway databases

BioCyciEcoCyc:PD03831

Miscellaneous databases

EvolutionaryTraceiP03004

Protein Ontology

More...
PROi
PR:P03004

Family and domain databases

CDDicd06571, Bac_DnaA_C, 1 hit
Gene3Di1.10.1750.10, 1 hit
3.30.300.180, 1 hit
HAMAPiMF_00377, DnaA_bact, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR001957, Chromosome_initiator_DnaA
IPR020591, Chromosome_initiator_DnaA-like
IPR018312, Chromosome_initiator_DnaA_CS
IPR013317, DnaA
IPR013159, DnaA_C
IPR024633, DnaA_N_dom
IPR038454, DnaA_N_sf
IPR027417, P-loop_NTPase
IPR010921, Trp_repressor/repl_initiator
PANTHERiPTHR30050:SF2, PTHR30050:SF2, 1 hit
PfamiView protein in Pfam
PF00308, Bac_DnaA, 1 hit
PF08299, Bac_DnaA_C, 1 hit
PF11638, DnaA_N, 1 hit
PRINTSiPR00051, DNAA
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SM00760, Bac_DnaA_C, 1 hit
SUPFAMiSSF48295, SSF48295, 1 hit
SSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00362, DnaA, 1 hit
PROSITEiView protein in PROSITE
PS01008, DNAA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDNAA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03004
Secondary accession number(s): P78122, Q2M814
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: April 7, 2021
This is version 190 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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