Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P16304 (KAD_BACSU)

Entry version 162 (08 May 2019)
Sequence version 2 (01 Feb 1991)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Adenylate kinase

Gene

adk

Organism
Bacillus subtilis (strain 168)
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

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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>Temperature dependencei

Optimum temperature is 45 degrees Celsius. Thermal denaturation midpoint (Tm) is 47.6 degrees Celsius and is raised to 66.0 degrees Celsius when AK is complexed with the inhibitor Ap5A.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from ADP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenylate kinase (adk)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from ADP, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei31AMPUniRule annotation2 Publications1
Binding sitei36AMPUniRule annotation2 Publications1
Binding sitei92AMPUniRule annotation2 Publications1
Binding sitei127ATPUniRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi130Zinc; structuralUniRule annotation2 Publications1
Metal bindingi133Zinc; structuralUniRule annotation2 Publications1
Metal bindingi150Zinc; structuralUniRule annotation2 Publications1
Metal bindingi153Zinc; structuralUniRule annotation2 Publications1
Binding sitei160AMPUniRule annotation2 Publications1
Binding sitei171AMPUniRule annotation2 Publications1
Binding sitei199ATP; via carbonyl oxygenUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi10 – 15ATPUniRule annotation2 Publications6
Nucleotide bindingi57 – 59AMPUniRule annotation2 Publications3
Nucleotide bindingi85 – 88AMPUniRule annotation2 Publications4
Nucleotide bindingi136 – 137ATPUniRule annotation2 Publications2

<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 functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		BSUB:BSU01370-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.4.3 658

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P16304

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00588;UER00649

<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_and_taxonomy_section">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:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Superoxide-inducible protein 16
Short name:
SOI16
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:adkUniRule annotation
Ordered Locus Names:BSU01370
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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

Complete GO annotation on QuickGO ...

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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB01717 Bis(Adenosine)-5'-Pentaphosphate

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001587301 – 217Adenylate kinaseAdd BLAST217

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P16304

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

More...PaxDbi		P16304

PRoteomics IDEntifications database

More...PRIDEi		P16304

<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

By superoxide.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P16304, 1 interactor

Molecular INTeraction database

More...MINTi		P16304

STRING: functional protein association networks

More...STRINGi		224308.BSU01370

<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

1217
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		P16304

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P16304

<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

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>Regioni30 – 59NMPbindUniRule annotation2 PublicationsAdd BLAST30
Regioni126 – 163LIDUniRule annotation2 PublicationsAdd BLAST38

<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

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.UniRule annotation3 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 adenylate kinase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0563 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000238772

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16304

KEGG Orthology (KO)

More...KOi		K00939

Identification of Orthologs from Complete Genome Data

More...OMAi		EKFTSQG

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16304

Family and domain databases

Conserved Domains Database

More...CDDi		cd01428 ADK, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00235 Adenylate_kinase_Adk, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006259 Adenyl_kin_sub
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR007862 Adenylate_kinase_lid-dom
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...PANTHERi		PTHR23359 PTHR23359, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF05191 ADK_lid, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00094 ADENYLTKNASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01351 adk, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00113 ADENYLATE_KINASE, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P16304-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLVLMGLPG AGKGTQGERI VEDYGIPHIS TGDMFRAAMK EETPLGLEAK 
        60         70         80         90        100
SYIDKGELVP DEVTIGIVKE RLGKDDCERG FLLDGFPRTV AQAEALEEIL 
       110        120        130        140        150
EEYGKPIDYV INIEVDKDVL MERLTGRRIC SVCGTTYHLV FNPPKTPGIC 
       160        170        180        190        200
DKDGGELYQR ADDNEETVSK RLEVNMKQTQ PLLDFYSEKG YLANVNGQQD 
       210 
IQDVYADVKD LLGGLKK
Length:217
Mass (Da):24,119
Last modified:February 1, 1991 - 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:iECB9ECF4F26A1E90
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
D00619 Genomic DNA Translation: BAA00496.1
L47971 Genomic DNA Translation: AAB06820.1
AL009126 Genomic DNA Translation: CAB11913.1
M31102 Genomic DNA Translation: AAB59119.1
X51329 Genomic DNA Translation: CAA35713.1

Protein sequence database of the Protein Information Resource

More...PIRi		JS0492

NCBI Reference Sequences

More...RefSeqi		NP_388018.1, NC_000964.3
WP_004399686.1, NZ_JNCM01000029.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB11913; CAB11913; BSU01370

Database of genes from NCBI RefSeq genomes

More...GeneIDi		938508

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU01370

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.140

<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
D00619 Genomic DNA Translation: BAA00496.1
L47971 Genomic DNA Translation: AAB06820.1
AL009126 Genomic DNA Translation: CAB11913.1
M31102 Genomic DNA Translation: AAB59119.1
X51329 Genomic DNA Translation: CAA35713.1
PIRiJS0492
RefSeqiNP_388018.1, NC_000964.3
WP_004399686.1, NZ_JNCM01000029.1

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
1P3JX-ray1.90A1-217[»]
2EU8X-ray1.80A/B1-216[»]
2OO7X-ray1.80A/B1-217[»]
2ORIX-ray1.80A/B1-216[»]
2OSBX-ray1.80A/B1-216[»]
2P3SX-ray1.80A1-217[»]
2QAJX-ray1.80A/B1-217[»]
3DKVX-ray1.82A1-217[»]
3DL0X-ray1.58A/B1-216[»]
4MKFX-ray1.70A/B1-217[»]
4MKGX-ray1.45A1-217[»]
4MKHX-ray1.50A1-212[»]
4QBFX-ray1.80A1-217[»]
4QBGX-ray1.37B1-217[»]
4TYPX-ray2.90A/B/C/D1-217[»]
4TYQX-ray1.65A/B1-217[»]
5X6IX-ray2.00A1-217[»]
SMRiP16304
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16304, 1 interactor
MINTiP16304
STRINGi224308.BSU01370

Chemistry databases

DrugBankiDB01717 Bis(Adenosine)-5'-Pentaphosphate

Proteomic databases

jPOSTiP16304
PaxDbiP16304
PRIDEiP16304

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11913; CAB11913; BSU01370
GeneIDi938508
KEGGibsu:BSU01370
PATRICifig|224308.179.peg.140

Phylogenomic databases

eggNOGiCOG0563 LUCA
HOGENOMiHOG000238772
InParanoidiP16304
KOiK00939
OMAiEKFTSQG
PhylomeDBiP16304

Enzyme and pathway databases

UniPathwayiUPA00588;UER00649
BioCyciBSUB:BSU01370-MONOMER
BRENDAi2.7.4.3 658
SABIO-RKiP16304

Miscellaneous databases

EvolutionaryTraceiP16304

Family and domain databases

CDDicd01428 ADK, 1 hit
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
InterProiView protein in InterPro
IPR006259 Adenyl_kin_sub
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR007862 Adenylate_kinase_lid-dom
IPR027417 P-loop_NTPase
PANTHERiPTHR23359 PTHR23359, 1 hit
PfamiView protein in Pfam
PF05191 ADK_lid, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01351 adk, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiKAD_BACSU
<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: P16304
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: May 8, 2019
This is version 162 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again