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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-Experimental evidence at protein leveli

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

Cofactori

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

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
    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
    Nucleotide bindingi116 – 119GTPUniRule annotation4
    Nucleotide bindingi171 – 179GTPUniRule annotation9

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BioCyciBSUB:BSU15780-MONOMER.

    Names & Taxonomyi

    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
    Gene namesi
    Name:rsgAUniRule annotation
    Synonyms:cpgA1 Publication, engC, yloQ1 Publication
    Ordered Locus Names:BSU15780
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    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
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001714641 – 298Small ribosomal subunit biogenesis GTPase RsgAAdd BLAST298

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei166Phosphothreonine1 Publication1

    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

    PaxDbiO34530.

    Interactioni

    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

    STRINGi224308.Bsubs1_010100008711.

    Structurei

    Secondary structure

    1298
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 10Combined sources8
    Beta strandi13 – 18Combined sources6
    Beta strandi20 – 23Combined sources4
    Beta strandi25 – 31Combined sources7
    Beta strandi47 – 51Combined sources5
    Beta strandi58 – 63Combined sources6
    Turni71 – 74Combined sources4
    Beta strandi80 – 87Combined sources8
    Turni88 – 91Combined sources4
    Helixi94 – 105Combined sources12
    Turni106 – 108Combined sources3
    Beta strandi110 – 116Combined sources7
    Helixi118 – 120Combined sources3
    Helixi124 – 140Combined sources17
    Beta strandi144 – 146Combined sources3
    Helixi149 – 152Combined sources4
    Turni156 – 158Combined sources3
    Helixi159 – 162Combined sources4
    Beta strandi165 – 172Combined sources8
    Helixi173 – 184Combined sources12
    Beta strandi211 – 214Combined sources4
    Beta strandi217 – 222Combined sources6
    Helixi235 – 238Combined sources4
    Helixi239 – 241Combined sources3
    Helixi243 – 248Combined sources6
    Helixi249 – 251Combined sources3
    Beta strandi259 – 261Combined sources3
    Helixi266 – 272Combined sources7
    Helixi278 – 292Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1T9HX-ray1.60A1-298[»]
    ProteinModelPortaliO34530.
    SMRiO34530.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO34530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini67 – 228CP-type GPROSITE-ProRule annotationAdd BLAST162

    Sequence similaritiesi

    Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105E06. Bacteria.
    COG1162. LUCA.
    HOGENOMiHOG000006958.
    InParanoidiO34530.
    KOiK06949.
    OMAiTHIIAAN.
    PhylomeDBiO34530.

    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. DUF258. 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.

    Sequencei

    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
    Checksum:iE58A69CAE570F855
    GO

    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.

    Genome annotation databases

    EnsemblBacteriaiCAB13451; CAB13451; BSU15780.
    GeneIDi938451.
    KEGGibsu:BSU15780.
    PATRICi18974963. VBIBacSub10457_1673.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1T9HX-ray1.60A1-298[»]
    ProteinModelPortaliO34530.
    SMRiO34530.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100008711.

    Proteomic databases

    PaxDbiO34530.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB13451; CAB13451; BSU15780.
    GeneIDi938451.
    KEGGibsu:BSU15780.
    PATRICi18974963. VBIBacSub10457_1673.

    Phylogenomic databases

    eggNOGiENOG4105E06. Bacteria.
    COG1162. LUCA.
    HOGENOMiHOG000006958.
    InParanoidiO34530.
    KOiK06949.
    OMAiTHIIAAN.
    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. DUF258. 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.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRSGA_BACSU
    AccessioniPrimary (citable) accession number: O34530
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: January 1, 1998
    Last modified: April 12, 2017
    This is version 117 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.