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UniProtKB - P21514 (PDEL_ECOLI)

Entry version 157 (23 Feb 2022)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Cyclic di-GMP phosphodiesterase PdeL

Gene

pdeL

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

Acts both as an enzyme and as a c-di-GMP sensor to couple transcriptional activity to the c-di-GMP status of the cell (PubMed:26553851).

Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (PubMed:15995192, PubMed:24451384, PubMed:26553851).

Also acts as a transcription factor to control its own expression (PubMed:26553851).

3 Publications

Miscellaneous

An overexpressed EAL domain (residues 77-362) has similar KM, Vmax, pH and metal dependence and subunit composition as the full-length protein.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+2 Publications, Mn2+1 Publication

<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

Strongly inhibited by Ca2+.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=25 µM for c-di-GMP1 Publication

pH dependencei

Optimum pH is 9.35.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei127SubstrateCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi141Magnesium or manganeseCombined sources1 Publication1
Metal bindingi200Magnesium or manganeseCombined sources1 Publication1
Binding sitei200SubstrateCombined sources1 Publication1
Metal bindingi232Magnesium or manganeseCombined sources1 Publication1
Metal bindingi262Magnesium or manganeseCombined sources1 Publication1
Binding sitei262SubstrateCombined sources1 Publication1
Binding sitei286SubstrateCombined sources1 Publication1
Binding sitei341SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi42 – 61H-T-H motifPROSITE-ProRule annotationAdd BLAST20

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: EcoCyc
Complete GO annotation on QuickGO ...

<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, Hydrolase
Biological processTranscription, Transcription regulation
Ligandc-di-GMP, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11236-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P21514

<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:
Cyclic di-GMP phosphodiesterase PdeLCurated (EC:3.1.4.523 Publications)
<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:pdeL1 Publication
Synonyms:yahA
Ordered Locus Names:b0315, JW0307
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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 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>Mutagenesisi60K → A: Does not bind to the PdeL box. 1 Publication1
Mutagenesisi206F → S: Increases catalytic activity. 1 Publication1
Mutagenesisi249F → L: Increases catalytic activity. 1 Publication1
Mutagenesisi263D → N: Loss of activity. 1 Publication1
Mutagenesisi298S → W: Slow monomer-dimer exchange. Equilibrium largely on the monomeric side, in particular in the presence of substrate. Strong decrease in activity. 1 Publication1
Mutagenesisi299G → S: Increases catalytic 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_00001685731 – 362Cyclic di-GMP phosphodiesterase PdeLAdd BLAST362

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P21514

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

More...PaxDbi		P21514

PRoteomics IDEntifications database

More...PRIDEi		P21514

<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

Autoregulated. Directly regulates its own expression in a c-di-GMP-dependent manner.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

Is in a fast thermodynamic monomer-homodimer equilibrium. Dimerization is required for PDE activity. Dimerization affinity is increased about 100-fold upon substrate binding.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262803, 8 interactors

Protein interaction database and analysis system

More...IntActi		P21514, 3 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0315

<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

1362
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		P21514

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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>Domaini18 – 83HTH luxR-typePROSITE-ProRule annotationAdd BLAST66
Domaini106 – 360EALPROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni144 – 145Substrate bindingCombined sources1 Publication2
Regioni319 – 322Substrate bindingCombined sources1 Publication4

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG2200, Bacteria
COG2771, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000445_70_50_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P21514

Database for complete collections of gene phylogenies

More...PhylomeDBi		P21514

Family and domain databases

Conserved Domains Database

More...CDDi		cd01948, EAL, 1 hit
cd06170, LuxR_C_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 1 hit
3.20.20.450, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001633, EAL_dom
IPR035919, EAL_sf
IPR016032, Sig_transdc_resp-reg_C-effctor
IPR000792, Tscrpt_reg_LuxR_C
IPR036388, WH-like_DNA-bd_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00563, EAL, 1 hit
PF00196, GerE, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00052, EAL, 1 hit
SM00421, HTH_LUXR, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF141868, SSF141868, 1 hit
SSF46894, SSF46894, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50883, EAL, 1 hit
PS50043, HTH_LUXR_2, 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.

P21514-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNSCDFRVFL QEFGTTVHLS LPGSVSEKER LLLKLLMQGM SVTEISQYRN 
        60         70         80         90        100
RSAKTISHQK KQLFEKLGIQ SDITFWRDIF FQYNPEIISA TGSNSHRYIN 
       110        120        130        140        150
DNHYHHIVTP EAISLALENH EFKPWIQPVF CAQTGVLTGC EVLVRWEHPQ 
       160        170        180        190        200
TGIIPPDQFI PLAESSGLIV IMTRQLMKQT ADILMPVKHL LPDNFHIGIN 
       210        220        230        240        250
VSAGCFLAAG FEKECLNLVN KLGNDKIKLV LELTERNPIP VTPEARAIFD 
       260        270        280        290        300
SLHQHNITFA LDDFGTGYAT YRYLQAFPVD FIKIDKSFVQ MASVDEISGH 
       310        320        330        340        350
IVDNIVELAR KPGLSIVAEG VETQEQADLM IGKGVHFLQG YLYSPPVPGN 
       360 
KFISEWVMKA GG
Length:362
Mass (Da):40,725
Last modified:November 1, 1997 - 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:i4BCA091840F27A0D
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 AAB18041 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U73857 Genomic DNA Translation: AAB18041.1 Different initiation.
U00096 Genomic DNA Translation: AAC73418.1
AP009048 Genomic DNA Translation: BAE76098.1
X52905 Genomic DNA Translation: CAA37089.1

Protein sequence database of the Protein Information Resource

More...PIRi		C64758

NCBI Reference Sequences

More...RefSeqi		NP_414849.1, NC_000913.3
WP_001301264.1, NZ_SSZK01000075.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73418; AAC73418; b0315
BAE76098; BAE76098; BAE76098

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947459

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0307
eco:b0315

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1962

<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
U73857 Genomic DNA Translation: AAB18041.1 Different initiation.
U00096 Genomic DNA Translation: AAC73418.1
AP009048 Genomic DNA Translation: BAE76098.1
X52905 Genomic DNA Translation: CAA37089.1
PIRiC64758
RefSeqiNP_414849.1, NC_000913.3
WP_001301264.1, NZ_SSZK01000075.1

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
4KIEX-ray1.70A96-362[»]
4LJ3X-ray1.70A/B101-362[»]
4LYKX-ray2.40A/B/C/D101-362[»]
SMRiP21514
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262803, 8 interactors
IntActiP21514, 3 interactors
STRINGi511145.b0315

Proteomic databases

jPOSTiP21514
PaxDbiP21514
PRIDEiP21514

Genome annotation databases

EnsemblBacteriaiAAC73418; AAC73418; b0315
BAE76098; BAE76098; BAE76098
GeneIDi947459
KEGGiecj:JW0307
eco:b0315
PATRICifig|1411691.4.peg.1962

Organism-specific databases

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

More...EchoBASEi		EB1218

Phylogenomic databases

eggNOGiCOG2200, Bacteria
COG2771, Bacteria
HOGENOMiCLU_000445_70_50_6
InParanoidiP21514
PhylomeDBiP21514

Enzyme and pathway databases

BioCyciEcoCyc:EG11236-MONOMER
SABIO-RKiP21514

Miscellaneous databases

Protein Ontology

More...PROi		PR:P21514

Family and domain databases

CDDicd01948, EAL, 1 hit
cd06170, LuxR_C_like, 1 hit
Gene3Di1.10.10.10, 1 hit
3.20.20.450, 1 hit
InterProiView protein in InterPro
IPR001633, EAL_dom
IPR035919, EAL_sf
IPR016032, Sig_transdc_resp-reg_C-effctor
IPR000792, Tscrpt_reg_LuxR_C
IPR036388, WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF00563, EAL, 1 hit
PF00196, GerE, 1 hit
SMARTiView protein in SMART
SM00052, EAL, 1 hit
SM00421, HTH_LUXR, 1 hit
SUPFAMiSSF141868, SSF141868, 1 hit
SSF46894, SSF46894, 1 hit
PROSITEiView protein in PROSITE
PS50883, EAL, 1 hit
PS50043, HTH_LUXR_2, 1 hit

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 nameiPDEL_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: P21514
Secondary accession number(s): P75689, Q2MCA8
<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: May 1, 1991
Last sequence update: November 1, 1997
Last modified: February 23, 2022
This is version 157 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
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