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Entry version 174 (07 Oct 2020)
Sequence version 2 (19 Jul 2003)
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Protein

Primosomal protein N'

Gene

priA

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

Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Is also involved in initiation of normal DNA replication in various plasmids and phages. Binds to branched DNA structures that resemble D-loops or to the primosome assembly site (PAS). Binds to DNA in two distinct modes, either dependent on or independent of the 3' terminus recognition.UniRule annotation10 Publications

<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

ATPase activity is stimulated by binding to DNA. Helicase activity is stimulated by SSB.3 Publications

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 bindingi224 – 231ATPUniRule annotation8
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri436 – 448C4-typeUniRule annotationAdd BLAST13
Zinc fingeri463 – 479C4-typeUniRule annotationAdd BLAST17

<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-binding, Helicase, Hydrolase
Biological processDNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10763-MONOMER
MetaCyc:EG10763-MONOMER

<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:
Primosomal protein N'UniRule annotation (EC:3.6.4.-UniRule annotation)
Alternative name(s):
ATP-dependent helicase PriAUniRule annotation
Replication factor Y
<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:priAUniRule annotation
Ordered Locus Names:b3935, JW3906
<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

GO - Cellular componenti

Keywords - Cellular componenti

Primosome

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutants show delayed replication restart after exposition to UV.1 Publication

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>Mutagenesisi226T → V: Strong decrease in ATPase and helicase activities. Does not affect DNA binding. 1 Publication1
Mutagenesisi230K → D: Lack of ATPase activity and strong decrease in helicase activity. Does not affect DNA binding. 2 Publications1
Mutagenesisi230K → R: Lack of helicase activity. Decreases Mu DNA replication. 2 Publications1
Mutagenesisi320D → A: Strong decrease in ATPase and helicase activities. Decreases DNA binding. 1 Publication1
Mutagenesisi584R → A: Does not affect DNA binding, but impairs ATPase activity. 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_00001021231 – 732Primosomal protein N'Add BLAST732

Proteomic databases

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

More...
PaxDbi
P17888

PRoteomics IDEntifications database

More...
PRIDEi
P17888

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by hydroxyurea.1 Publication

<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

Component of the primosome, which is composed of PriA, PriB, PriC, DnaB, DnaC, DnaG and DnaT. Binds ssDNA as a monomer.

Interacts with SSB and PriB.

UniRule annotation4 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262651, 65 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1951, DnaB-DnaC-DnaT-PriA-PriB complex
CPX-1952, DnaB-DnaC-DnaT-PriA-PriC complex

Database of interacting proteins

More...
DIPi
DIP-10562N

Protein interaction database and analysis system

More...
IntActi
P17888, 17 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3935

<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

1732
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
P17888

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
P17888

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini211 – 377Helicase ATP-bindingUniRule annotationAdd BLAST167
Domaini447 – 638Helicase C-terminalUniRule annotationAdd BLAST192

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi320 – 323DEAH box4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an N-terminal DNA-binding domain and a C-terminal helicase domain. The helicase domain plays an important role in high affinity and stable binding of PriA to forked DNAs.2 Publications

<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 helicase family. PriA subfamily.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri436 – 448C4-typeUniRule annotationAdd BLAST13
Zinc fingeri463 – 479C4-typeUniRule annotationAdd BLAST17

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1198, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013353_3_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17888

KEGG Orthology (KO)

More...
KOi
K04066

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P17888

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.8.630, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00983, PriA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR005259, PriA
IPR041222, PriA_3primeBD
IPR042115, PriA_3primeBD_sf
IPR041236, PriA_C
IPR040498, PriA_CRR

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit
PF17764, PriA_3primeBD, 1 hit
PF18074, PriA_C, 1 hit
PF18319, PriA_CRR, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00595, priA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 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.

P17888-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVAHVALPV PLPRTFDYLL PEGMTVKAGC RVRVPFGKQQ ERIGIVVSVS
60 70 80 90 100
DASELPLNEL KAVVEVLDSE PVFTHSVWRL LLWAADYYHH PIGDVLFHAL
110 120 130 140 150
PILLRQGRPA ANAPMWYWFA TEQGQAVDLN SLKRSPKQQQ ALAALRQGKI
160 170 180 190 200
WRDQVATLEF NDAALQALRK KGLCDLASET PEFSDWRTNY AVSGERLRLN
210 220 230 240 250
TEQATAVGAI HSAADTFSAW LLAGVTGSGK TEVYLSVLEN VLAQGKQALV
260 270 280 290 300
MVPEIGLTPQ TIARFRERFN APVEVLHSGL NDSERLSAWL KAKNGEAAIV
310 320 330 340 350
IGTRSALFTP FKNLGVIVID EEHDSSYKQQ EGWRYHARDL AVYRAHSEQI
360 370 380 390 400
PIILGSATPA LETLCNVQQK KYRLLRLTRR AGNARPAIQH VLDLKGQKVQ
410 420 430 440 450
AGLAPALITR MRQHLQADNQ VILFLNRRGF APALLCHDCG WIAECPRCDH
460 470 480 490 500
YYTLHQAQHH LRCHHCDSQR PVPRQCPSCG STHLVPVGLG TEQLEQTLAP
510 520 530 540 550
LFPGVPISRI DRDTTSRKGA LEQQLAEVHR GGARILIGTQ MLAKGHHFPD
560 570 580 590 600
VTLVALLDVD GALFSADFRS AERFAQLYTQ VAGRAGRAGK QGEVVLQTHH
610 620 630 640 650
PEHPLLQTLL YKGYDAFAEQ ALAERRMMQL PPWTSHVIVR AEDHNNQHAP
660 670 680 690 700
LFLQQLRNLI LSSPLADEKL WVLGPVPALA PKRGGRWRWQ ILLQHPSRVR
710 720 730
LQHIINGTLA LINTIPDSRK VKWVLDVDPI EG
Length:732
Mass (Da):81,655
Last modified:July 19, 2003 - 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:iAB6C90F43042A363
GO

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 conflicti156A → R in AAA24416 (PubMed:2162050).Curated1
Sequence conflicti621A → R in AAA24416 (PubMed:2162050).Curated1
Sequence conflicti649A → V in BAA00491 (PubMed:2162049).Curated1

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
M33293 Genomic DNA Translation: AAA24416.1
D00616 Genomic DNA Translation: BAA00491.1
L19201 Genomic DNA Translation: AAB03067.1
U00096 Genomic DNA Translation: AAC76917.1
AP009048 Genomic DNA Translation: BAE77375.1

Protein sequence database of the Protein Information Resource

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PIRi
S40878, A35505

NCBI Reference Sequences

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RefSeqi
NP_418370.1, NC_000913.3
WP_001301269.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76917; AAC76917; b3935
BAE77375; BAE77375; BAE77375

Database of genes from NCBI RefSeq genomes

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GeneIDi
948426

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3906
eco:b3935

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2770

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
M33293 Genomic DNA Translation: AAA24416.1
D00616 Genomic DNA Translation: BAA00491.1
L19201 Genomic DNA Translation: AAB03067.1
U00096 Genomic DNA Translation: AAC76917.1
AP009048 Genomic DNA Translation: BAE77375.1
PIRiS40878, A35505
RefSeqiNP_418370.1, NC_000913.3
WP_001301269.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D7EX-ray2.50A/B/C/D1-105[»]
2D7GX-ray3.30A/B/C/D1-105[»]
2D7HX-ray3.00A/B/C/D1-105[»]
2DWLX-ray3.20A/B/C/D1-105[»]
2DWMX-ray3.15A/B/C/D1-105[»]
2DWNX-ray3.35A/B/C/D1-105[»]
6DCRX-ray1.98A/B1-114[»]
A/B175-732[»]
SMRiP17888
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262651, 65 interactors
ComplexPortaliCPX-1951, DnaB-DnaC-DnaT-PriA-PriB complex
CPX-1952, DnaB-DnaC-DnaT-PriA-PriC complex
DIPiDIP-10562N
IntActiP17888, 17 interactors
STRINGi511145.b3935

Proteomic databases

PaxDbiP17888
PRIDEiP17888

Genome annotation databases

EnsemblBacteriaiAAC76917; AAC76917; b3935
BAE77375; BAE77375; BAE77375
GeneIDi948426
KEGGiecj:JW3906
eco:b3935
PATRICifig|1411691.4.peg.2770

Organism-specific databases

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

More...
EchoBASEi
EB0756

Phylogenomic databases

eggNOGiCOG1198, Bacteria
HOGENOMiCLU_013353_3_1_6
InParanoidiP17888
KOiK04066
PhylomeDBiP17888

Enzyme and pathway databases

BioCyciEcoCyc:EG10763-MONOMER
MetaCyc:EG10763-MONOMER

Miscellaneous databases

EvolutionaryTraceiP17888

Protein Ontology

More...
PROi
PR:P17888

Family and domain databases

Gene3Di1.10.8.630, 1 hit
HAMAPiMF_00983, PriA, 1 hit
InterProiView protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR005259, PriA
IPR041222, PriA_3primeBD
IPR042115, PriA_3primeBD_sf
IPR041236, PriA_C
IPR040498, PriA_CRR
PfamiView protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit
PF17764, PriA_3primeBD, 1 hit
PF18074, PriA_C, 1 hit
PF18319, PriA_CRR, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00595, priA, 1 hit
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPRIA_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: P17888
Secondary accession number(s): Q2M8N1
<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: November 1, 1990
Last sequence update: July 19, 2003
Last modified: October 7, 2020
This is version 174 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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