Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 135 (25 May 2022)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Small ribosomal subunit biogenesis GTPase RsgA

Gene

rsgA

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

One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP (PubMed:16485133).

GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation (PubMed:22544754).

Depletion results in increased sensitivity to protein synthesis inhibitors that block the peptide channel or peptidyl transferase center on the ribosome, suggesting this protein functions in conjunction with the ribosome in vivo (PubMed:15828870).

Decreasing levels of protein lead to an increase in free 30S and 50S ribosomal subunits and a decrease in assembled 70S ribosomes (PubMed:15828870).

Suggested to serve as a specific transcription factor for proteins involved in late stages of peptidoglycan synthesis (PubMed:18344364).

4 Publications

<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

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 Publication

<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

kcat for GTP is 13.6 h(-1), in the absence of ribosomes.1 Publication
  1. KM=30.5 µM for GTP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi252ZincUniRule annotation1 Publication1
Metal bindingi257ZincUniRule annotation1 Publication1
Metal bindingi259Zinc; via pros nitrogenUniRule annotation1 Publication1
Metal bindingi265ZincUniRule annotation1 Publication1

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 bindingi116 – 119GTPUniRule annotation4
Nucleotide bindingi171 – 179GTPUniRule annotation9

<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 functionHydrolase, RNA-binding, rRNA-binding
Biological processRibosome biogenesis
LigandGTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU15780-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:
Small ribosomal subunit biogenesis GTPase RsgAUniRule annotation (EC:3.6.1.-UniRule annotation1 Publication)
Alternative name(s):
Ribosome-associated GTPase CpgA1 Publication
<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:rsgAUniRule annotation
Synonyms:cpgA1 Publication, engC, yloQ1 Publication
Ordered Locus Names:BSU15780
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

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

Keywords - Cellular componenti

Cytoplasm

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

<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

Has been described as essential (PubMed:9743119, PubMed:16485133, PubMed:18344364), but also as non-essential (PubMed:15828870). Cells have a slow growth phenotype (PubMed:15828870, PubMed:16485133, PubMed:18344364, PubMed:22544754). Disrupted strain grows as chains of filaments, a cell curvature phenotype is also present, resulting in long wavy cells or short curved rods (PubMed:15828870, PubMed:22544754). Depleted cells form aberrant, swollen cells (PubMed:16485133, PubMed:18344364). Depleted cells DNA staining shows fragmented and/or disturbed nucleoid segregation; effects are seen most in minimal E-medium (PubMed:16485133). Depleted cells have an irregular deposition of cell wall and 15% have abnormal septal cleavage planes (PubMed:18344364).4 Publications

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>Mutagenesisi166T → A: Loss of most phosphorylation by PrkC, GTPase activity less stimulated by 70S ribosomes than wild-type, decreased association with 30S ribosomal subunit in vitro. Grows slowly, cells have abnormal morphology. 1 Publication1
Mutagenesisi166T → D: Higher endogenous GTPase activity, GTPase more stimulated by 70S ribosomes than wild-type, increased association with 30S ribosomal subunit in vitro, wild-type behavior in vivo. 1 Publication1
Mutagenesisi177K → A: Grows slowly, cells have abnormal morphology. 1 Publication1
Mutagenesisi178S → A: No GTPase activity. Wild-type phosphorylation by PrkC in vitro. 1 Publication1
Mutagenesisi192T → A: Loss of phosphorylation by PrkC, but PrkC autophosphorylation greatly decreased in vitro. 1 Publication1
Mutagenesisi196S → A: Wild-type phosphorylation by PrkC in vitro. 1 Publication1
Mutagenesisi206T → A: Wild-type phosphorylation by PrkC in vitro. 1 Publication1
Mutagenesisi222T → A: Wild-type phosphorylation by PrkC in vitro. 1 Publication1
Mutagenesisi226S → A: Loss of phosphorylation by PrkC, but PrkC autophosphorylation considerably decreased in vitro. 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_00001714641 – 298Small ribosomal subunit biogenesis GTPase RsgAAdd BLAST298

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 residuei166Phosphothreonine1 Publication1

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

In vitro phosphorylated mostly on Thr (with lower signal on Ser) by PrkC in the presence of poly-L-Lys or myelin basic protein, dephosphorylated by PrpC (PubMed:19246764). Most in vitro phosphorylation occurs on Thr-166, in vivo phosphorylation has not been detected, but it might vary during the cell cycle (PubMed:22544754).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O34530

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

More...
PaxDbi
O34530

PRoteomics IDEntifications database

More...
PRIDEi
O34530

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O34530

<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

Monomer, but able to form dimers (PubMed:16485133). Associates with 30S ribosomal subunit; a phospho-mimetic mutation increases association (PubMed:22544754). Probably binds 16S rRNA.

1 Publication2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU15780

<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

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
O34530

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

More...
SMRi
O34530

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
O34530

<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>Domaini67 – 228CP-type GPROSITE-ProRule annotationAdd BLAST162

<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 TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1162, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O34530

Identification of Orthologs from Complete Genome Data

More...
OMAi
CLVAAYD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O34530

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04466, S1_YloQ_GTPase, 1 hit
cd01854, YjeQ_EngC, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.50.140, 1 hit
3.40.50.300, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01820, GTPase_RsgA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR030378, G_CP_dom
IPR012340, NA-bd_OB-fold
IPR027417, P-loop_NTPase
IPR004881, Ribosome_biogen_GTPase_RsgA
IPR010914, RsgA_GTPase_dom
IPR031944, RsgA_N

The PANTHER Classification System

More...
PANTHERi
PTHR32120, PTHR32120, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03193, RsgA_GTPase, 1 hit
PF16745, RsgA_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249, SSF50249, 1 hit
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00157, TIGR00157, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50936, ENGC_GTPASE, 1 hit
PS51721, G_CP, 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.

O34530-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEGKIIKAL SGFYYVLDES EDSDKVIQCR GRGIFRKNKI TPLVGDYVVY
60 70 80 90 100
QAENDKEGYL MEIKERTNEL IRPPICNVDQ AVLVFSAVQP SFSTALLDRF
110 120 130 140 150
LVLVEANDIQ PIICITKMDL IEDQDTEDTI QAYAEDYRNI GYDVYLTSSK
160 170 180 190 200
DQDSLADIIP HFQDKTTVFA GQSGVGKSSL LNAISPELGL RTNEISEHLG
210 220 230 240 250
RGKHTTRHVE LIHTSGGLVA DTPGFSSLEF TDIEEEELGY TFPDIREKSS
260 270 280 290
SCKFRGCLHL KEPKCAVKQA VEDGELKQYR YDHYVEFMTE IKDRKPRY
Length:298
Mass (Da):33,797
Last modified:January 1, 1998 - 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:iE58A69CAE570F855
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
Y13937 Genomic DNA Translation: CAA74251.1
AL009126 Genomic DNA Translation: CAB13451.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A69879

NCBI Reference Sequences

More...
RefSeqi
NP_389460.1, NC_000964.3
WP_003232060.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB13451; CAB13451; BSU_15780

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
938451

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU15780

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.1718

<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
Y13937 Genomic DNA Translation: CAA74251.1
AL009126 Genomic DNA Translation: CAB13451.1
PIRiA69879
RefSeqiNP_389460.1, NC_000964.3
WP_003232060.1, NZ_JNCM01000035.1

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
1T9HX-ray1.60A1-298[»]
AlphaFoldDBiO34530
SMRiO34530
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU15780

PTM databases

iPTMnetiO34530

Proteomic databases

jPOSTiO34530
PaxDbiO34530
PRIDEiO34530

Genome annotation databases

EnsemblBacteriaiCAB13451; CAB13451; BSU_15780
GeneIDi938451
KEGGibsu:BSU15780
PATRICifig|224308.179.peg.1718

Phylogenomic databases

eggNOGiCOG1162, Bacteria
InParanoidiO34530
OMAiCLVAAYD
PhylomeDBiO34530

Enzyme and pathway databases

BioCyciBSUB:BSU15780-MONOMER

Miscellaneous databases

EvolutionaryTraceiO34530

Family and domain databases

CDDicd04466, S1_YloQ_GTPase, 1 hit
cd01854, YjeQ_EngC, 1 hit
Gene3Di2.40.50.140, 1 hit
3.40.50.300, 1 hit
HAMAPiMF_01820, GTPase_RsgA, 1 hit
InterProiView protein in InterPro
IPR030378, G_CP_dom
IPR012340, NA-bd_OB-fold
IPR027417, P-loop_NTPase
IPR004881, Ribosome_biogen_GTPase_RsgA
IPR010914, RsgA_GTPase_dom
IPR031944, RsgA_N
PANTHERiPTHR32120, PTHR32120, 1 hit
PfamiView protein in Pfam
PF03193, RsgA_GTPase, 1 hit
PF16745, RsgA_N, 1 hit
SUPFAMiSSF50249, SSF50249, 1 hit
SSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00157, TIGR00157, 1 hit
PROSITEiView protein in PROSITE
PS50936, ENGC_GTPASE, 1 hit
PS51721, G_CP, 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 nameiRSGA_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: O34530
<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: October 31, 2003
Last sequence update: January 1, 1998
Last modified: May 25, 2022
This is version 135 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
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