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UniProtKB - O34530 (RSGA_BACSU)

Entry version 124 (08 May 2019)
Sequence version 1 (01 Jan 1998)
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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 hour(-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_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 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_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 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

    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 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_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:
    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_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: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_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

    <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_and_biotech_section">'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.<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_processing_section">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_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, 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

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

    More...    SMRi    		O34530

    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    		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_and_domains_section">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    		ENOG4105E06 Bacteria
    COG1162 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000006958

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		O34530

    KEGG Orthology (KO)

    More...    KOi    		K06949

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		FRDCKHL

    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

    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_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.

    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; BSU15780

    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[»]
    SMRiO34530
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.BSU15780

    PTM databases

    iPTMnetiO34530

    Proteomic databases

    jPOSTiO34530
    PaxDbiO34530
    PRIDEiO34530

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiENOG4105E06 Bacteria
    COG1162 LUCA
    HOGENOMiHOG000006958
    InParanoidiO34530
    KOiK06949
    OMAiFRDCKHL
    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
    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

    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 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_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: October 31, 2003
    Last sequence update: January 1, 1998
    Last modified: May 8, 2019
    This is version 124 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, Complete proteome, 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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