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UniProtKB - P0DMC7 (RCSB_ECOLI)

Entry version 59 (02 Jun 2021)
Sequence version 1 (19 Feb 2014)
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Protein

Transcriptional regulatory protein RcsB

Gene

rcsB

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

Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.

UniRule annotation7 Publications

Miscellaneous

There is a close linkage between the Rcs and PhoQ/P signaling systems, and both signaling systems respond to certain external divalent cations (zinc and magnesium).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

Activity is modulated by phosphorylation and interaction with other transcriptional regulators. Probably up-regulated by YmgA/AriR, and possibly down-regulated by YcgZ, all 3 are connector proteins providing additional signal input into the signaling system.2 Publications

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 bindingi168 – 187H-T-H motifUniRule 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

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 functionActivator, DNA-binding
Biological processCapsule biogenesis/degradation, Transcription, Transcription regulation, Two-component regulatory system

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RCSB-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:
Transcriptional regulatory protein RcsBUniRule annotation
Alternative name(s):
Capsular synthesis regulator component B
<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:rcsBUniRule annotation
Ordered Locus Names:b2217, JW2205
<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 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

<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>Mutagenesisi56D → E: Increases heterodimer formation with RcsA. Does not affect heterodimer formation with BglJ. 1 Publication1
Mutagenesisi56D → N: Decreases heterodimer formation with RcsA. Does not affect heterodimer formation with BglJ. 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_00000812091 – 216Transcriptional regulatory protein RcsBAdd BLAST216

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 residuei564-aspartylphosphateUniRule annotation1

<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

Phosphorylated and activated by RcsD.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0DMC7

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

More...PaxDbi		P0DMC7

PRoteomics IDEntifications database

More...PRIDEi		P0DMC7

<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

Expression is dependent on the alternate sigma factor, RpoN (PubMed:2404948). Repressed by hydroxyurea.2 Publications

<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

Interacts with RcsD and RcsA. Homodimer. Can form an heterodimer with the coactivator RcsA, which binds to the RcsAB boxes to promote transcription of RcsA-dependent genes. Can also form a heterodimer with GadE to bind to the GAD box, and with BglJ to bind to the bgl promoter.

UniRule annotation6 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260879, 5 interactors
851761, 4 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5762, rcsAB DNA-binding transcription factor complex
CPX-5763, bglJ-rcsB DNA-binding transcription factor complex
CPX-5764, matA-rcsB DNA-binding transcription factor complex
CPX-5765, rcsB DNA-binding transcription factor homodimer
CPX-5781, gadE-rcsB DNA-binding transcription factor complex

Protein interaction database and analysis system

More...IntActi		P0DMC7, 43 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2217

<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

1216
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		P0DMC7

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>Domaini5 – 124Response regulatoryPROSITE-ProRule annotationAdd BLAST120
Domaini144 – 209HTH luxR-typeUniRule annotationAdd BLAST66

<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 RcsB family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG2197, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000445_90_1_6

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0DMC7

Family and domain databases

Conserved Domains Database

More...CDDi		cd06170, LuxR_C_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00981, RcsB, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011006, CheY-like_superfamily
IPR030864, RcsB
IPR016032, Sig_transdc_resp-reg_C-effctor
IPR001789, Sig_transdc_resp-reg_receiver
IPR000792, Tscrpt_reg_LuxR_C
IPR036388, WH-like_DNA-bd_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00196, GerE, 1 hit
PF00072, Response_reg, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00038, HTHLUXR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00421, HTH_LUXR, 1 hit
SM00448, REC, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46894, SSF46894, 1 hit
SSF52172, SSF52172, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00622, HTH_LUXR_1, 1 hit
PS50043, HTH_LUXR_2, 1 hit
PS50110, RESPONSE_REGULATORY, 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.

P0DMC7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNNMNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINNLPKLDA 
        60         70         80         90        100
HVLITDLSMP GDKYGDGITL IKYIKRHFPS LSIIVLTMNN NPAILSAVLD 
       110        120        130        140        150
LDIEGIVLKQ GAPTDLPKAL AALQKGKKFT PESVSRLLEK ISAGGYGDKR 
       160        170        180        190        200
LSPKESEVLR LFAEGFLVTE IAKKLNRSIK TISSQKKSAM MKLGVENDIA 
       210 
LLNYLSSVTL SPADKD
Length:216
Mass (Da):23,671
Last modified:February 19, 2014 - v1
<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:iA78D1BD3004E0680
GO

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
M28242 Genomic DNA Translation: AAA24504.1
U00096 Genomic DNA Translation: AAC75277.1
AP009048 Genomic DNA Translation: BAA16000.1
S37760 Genomic DNA Translation: AAB22290.1

Protein sequence database of the Protein Information Resource

More...PIRi		JV0068, BVECCB

NCBI Reference Sequences

More...RefSeqi		NP_416721.1, NC_000913.3
WP_001061917.1, NZ_STEB01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75277; AAC75277; b2217
BAA16000; BAA16000; BAA16000

Database of genes from NCBI RefSeq genomes

More...GeneIDi		62016781
947441

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2205
eco:b2217

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.18

<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
M28242 Genomic DNA Translation: AAA24504.1
U00096 Genomic DNA Translation: AAC75277.1
AP009048 Genomic DNA Translation: BAA16000.1
S37760 Genomic DNA Translation: AAB22290.1
PIRiJV0068, BVECCB
RefSeqiNP_416721.1, NC_000913.3
WP_001061917.1, NZ_STEB01000002.1

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
5I4CX-ray2.00A1-147[»]
5VXNX-ray3.38A/B/C/D1-216[»]
5W43X-ray3.15A/B1-216[»]
SMRiP0DMC7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260879, 5 interactors
851761, 4 interactors
ComplexPortaliCPX-5762, rcsAB DNA-binding transcription factor complex
CPX-5763, bglJ-rcsB DNA-binding transcription factor complex
CPX-5764, matA-rcsB DNA-binding transcription factor complex
CPX-5765, rcsB DNA-binding transcription factor homodimer
CPX-5781, gadE-rcsB DNA-binding transcription factor complex
IntActiP0DMC7, 43 interactors
STRINGi511145.b2217

Proteomic databases

jPOSTiP0DMC7
PaxDbiP0DMC7
PRIDEiP0DMC7

Genome annotation databases

EnsemblBacteriaiAAC75277; AAC75277; b2217
BAA16000; BAA16000; BAA16000
GeneIDi62016781
947441
KEGGiecj:JW2205
eco:b2217
PATRICifig|1411691.4.peg.18

Organism-specific databases

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

More...EchoBASEi		EB0814

Phylogenomic databases

eggNOGiCOG2197, Bacteria
HOGENOMiCLU_000445_90_1_6
PhylomeDBiP0DMC7

Enzyme and pathway databases

BioCyciEcoCyc:RCSB-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P0DMC7

Family and domain databases

CDDicd06170, LuxR_C_like, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_00981, RcsB, 1 hit
InterProiView protein in InterPro
IPR011006, CheY-like_superfamily
IPR030864, RcsB
IPR016032, Sig_transdc_resp-reg_C-effctor
IPR001789, Sig_transdc_resp-reg_receiver
IPR000792, Tscrpt_reg_LuxR_C
IPR036388, WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF00196, GerE, 1 hit
PF00072, Response_reg, 1 hit
PRINTSiPR00038, HTHLUXR
SMARTiView protein in SMART
SM00421, HTH_LUXR, 1 hit
SM00448, REC, 1 hit
SUPFAMiSSF46894, SSF46894, 1 hit
SSF52172, SSF52172, 1 hit
PROSITEiView protein in PROSITE
PS00622, HTH_LUXR_1, 1 hit
PS50043, HTH_LUXR_2, 1 hit
PS50110, RESPONSE_REGULATORY, 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 nameiRCSB_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: P0DMC7
Secondary accession number(s): P14374, P69407
<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: February 19, 2014
Last sequence update: February 19, 2014
Last modified: June 2, 2021
This is version 59 of the entry and version 1 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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