RSGA_BACSU
ID RSGA_BACSU Reviewed; 298 AA.
AC O34530;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:16485133};
DE AltName: Full=Ribosome-associated GTPase CpgA {ECO:0000303|PubMed:22544754};
GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820};
GN Synonyms=cpgA {ECO:0000303|PubMed:16485133}, engC,
GN yloQ {ECO:0000303|PubMed:9534248}; OrderedLocusNames=BSU15780;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=9743119; DOI=10.1038/nbt0998-851;
RA Arigoni F., Talabot F., Peitsch M.C., Edgerton M.D., Meldrum E., Allet E.,
RA Fish R., Jamotte T., Curchod M.-L., Loferer H.;
RT "A genome-based approach for the identification of essential bacterial
RT genes.";
RL Nat. Biotechnol. 16:851-856(1998).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CHEMICAL SYNTHETIC LETHALITY.
RC STRAIN=168 / EB6;
RX PubMed=15828870; DOI=10.1042/bj20041873;
RA Campbell T.L., Daigle D.M., Brown E.D.;
RT "Characterization of the Bacillus subtilis GTPase YloQ and its role in
RT ribosome function.";
RL Biochem. J. 389:843-852(2005).
RN [5]
RP FUNCTION AS A GTPASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF SER-178.
RC STRAIN=168;
RX PubMed=16485133; DOI=10.1007/s00438-006-0097-9;
RA Cladiere L., Hamze K., Madec E., Levdikov V.M., Wilkinson A.J.,
RA Holland I.B., Seror S.J.;
RT "The GTPase, CpgA(YloQ), a putative translation factor, is implicated in
RT morphogenesis in Bacillus subtilis.";
RL Mol. Genet. Genomics 275:409-420(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=18344364; DOI=10.1128/jb.01994-07;
RA Absalon C., Hamze K., Blanot D., Frehel C., Carballido-Lopez R.,
RA Holland B.I., van Heijenoort J., Seror S.J.;
RT "The GTPase CpgA is implicated in the deposition of the peptidoglycan
RT sacculus in Bacillus subtilis.";
RL J. Bacteriol. 190:3786-3790(2008).
RN [7]
RP PHOSPHORYLATION AT SER AND THR, AND MUTAGENESIS OF SER-178; THR-192;
RP SER-196; THR-206; THR-222 AND SER-226.
RC STRAIN=168;
RX PubMed=19246764; DOI=10.1099/mic.0.022475-0;
RA Absalon C., Obuchowski M., Madec E., Delattre D., Holland I.B., Seror S.J.;
RT "CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr
RT kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.";
RL Microbiology 155:932-943(2009).
RN [8]
RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT THR-166, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF THR-166 AND LYS-177.
RC STRAIN=168;
RX PubMed=22544754; DOI=10.1074/jbc.m112.340331;
RA Pompeo F., Freton C., Wicker-Planquart C., Grangeasse C., Jault J.M.,
RA Galinier A.;
RT "Phosphorylation of CpgA protein enhances both its GTPase activity and its
RT affinity for ribosome and is crucial for Bacillus subtilis growth and
RT morphology.";
RL J. Biol. Chem. 287:20830-20838(2012).
RN [9] {ECO:0007744|PDB:1T9H}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP PROBABLE SUBUNIT.
RX PubMed=15223319; DOI=10.1016/j.jmb.2004.05.029;
RA Levdikov V.M., Blagova E.V., Brannigan J.A., Cladiere L., Antson A.A.,
RA Isupov M.N., Seror S.J., Wilkinson A.J.;
RT "The crystal structure of YloQ, a circularly permuted GTPase essential for
RT Bacillus subtilis viability.";
RL J. Mol. Biol. 340:767-782(2004).
CC -!- FUNCTION: One of several proteins that assist in the late maturation
CC steps of the functional core of the 30S ribosomal subunit. Helps
CC release RbfA from mature subunits. May play a role in the assembly of
CC ribosomal proteins into the subunit. Circularly permuted GTPase with a
CC low level of activity and slow catalytic turnover, does not act on ATP
CC (PubMed:16485133). GTPase activity is stimulated by the presence of 30S
CC or 70S ribosomes, phosphorylation increases stimulation
CC (PubMed:22544754). Depletion results in increased sensitivity to
CC protein synthesis inhibitors that block the peptide channel or peptidyl
CC transferase center on the ribosome, suggesting this protein functions
CC in conjunction with the ribosome in vivo (PubMed:15828870). Decreasing
CC levels of protein lead to an increase in free 30S and 50S ribosomal
CC subunits and a decrease in assembled 70S ribosomes (PubMed:15828870).
CC Suggested to serve as a specific transcription factor for proteins
CC involved in late stages of peptidoglycan synthesis (PubMed:18344364).
CC {ECO:0000269|PubMed:15828870, ECO:0000269|PubMed:16485133,
CC ECO:0000269|PubMed:18344364, ECO:0000269|PubMed:22544754}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:15223319};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:15223319};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30.5 uM for GTP {ECO:0000269|PubMed:16485133};
CC Note=kcat for GTP is 13.6 h(-1), in the absence of ribosomes.
CC {ECO:0000269|PubMed:16485133};
CC -!- SUBUNIT: Monomer, but able to form dimers (PubMed:16485133). Associates
CC with 30S ribosomal subunit; a phospho-mimetic mutation increases
CC association (PubMed:22544754). Probably binds 16S rRNA.
CC {ECO:0000269|PubMed:16485133, ECO:0000269|PubMed:22544754,
CC ECO:0000305|PubMed:15223319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- PTM: In vitro phosphorylated mostly on Thr (with lower signal on Ser)
CC by PrkC in the presence of poly-L-Lys or myelin basic protein,
CC dephosphorylated by PrpC (PubMed:19246764). Most in vitro
CC phosphorylation occurs on Thr-166, in vivo phosphorylation has not been
CC detected, but it might vary during the cell cycle (PubMed:22544754).
CC {ECO:0000269|PubMed:19246764, ECO:0000269|PubMed:22544754}.
CC -!- DISRUPTION PHENOTYPE: Has been described as essential (PubMed:9743119,
CC PubMed:16485133, PubMed:18344364), but also as non-essential
CC (PubMed:15828870). Cells have a slow growth phenotype (PubMed:15828870,
CC PubMed:16485133, PubMed:18344364, PubMed:22544754). Disrupted strain
CC grows as chains of filaments, a cell curvature phenotype is also
CC present, resulting in long wavy cells or short curved rods
CC (PubMed:15828870, PubMed:22544754). Depleted cells form aberrant,
CC swollen cells (PubMed:16485133, PubMed:18344364). Depleted cells DNA
CC staining shows fragmented and/or disturbed nucleoid segregation;
CC effects are seen most in minimal E-medium (PubMed:16485133). Depleted
CC cells have an irregular deposition of cell wall and 15% have abnormal
CC septal cleavage planes (PubMed:18344364). {ECO:0000269|PubMed:15828870,
CC ECO:0000269|PubMed:16485133, ECO:0000269|PubMed:18344364,
CC ECO:0000269|PubMed:9743119}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000305}.
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DR EMBL; Y13937; CAA74251.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13451.1; -; Genomic_DNA.
DR PIR; A69879; A69879.
DR RefSeq; NP_389460.1; NC_000964.3.
DR RefSeq; WP_003232060.1; NZ_JNCM01000035.1.
DR PDB; 1T9H; X-ray; 1.60 A; A=1-298.
DR PDBsum; 1T9H; -.
DR AlphaFoldDB; O34530; -.
DR SMR; O34530; -.
DR STRING; 224308.BSU15780; -.
DR iPTMnet; O34530; -.
DR jPOST; O34530; -.
DR PaxDb; O34530; -.
DR PRIDE; O34530; -.
DR EnsemblBacteria; CAB13451; CAB13451; BSU_15780.
DR GeneID; 938451; -.
DR KEGG; bsu:BSU15780; -.
DR PATRIC; fig|224308.179.peg.1718; -.
DR eggNOG; COG1162; Bacteria.
DR InParanoid; O34530; -.
DR OMA; CLVAAYD; -.
DR PhylomeDB; O34530; -.
DR BioCyc; BSUB:BSU15780-MON; -.
DR EvolutionaryTrace; O34530; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd04466; S1_YloQ_GTPase; 1.
DR CDD; cd01854; YjeQ_EngC; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01820; GTPase_RsgA; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR InterPro; IPR010914; RsgA_GTPase_dom.
DR InterPro; IPR031944; RsgA_N.
DR PANTHER; PTHR32120; PTHR32120; 1.
DR Pfam; PF03193; RsgA_GTPase; 1.
DR Pfam; PF16745; RsgA_N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00157; TIGR00157; 1.
DR PROSITE; PS50936; ENGC_GTPASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..298
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000171464"
FT DOMAIN 67..228
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 171..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15223319"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15223319"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15223319"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15223319"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22544754"
FT MUTAGEN 166
FT /note="T->A: Loss of most phosphorylation by PrkC, GTPase
FT activity less stimulated by 70S ribosomes than wild-type,
FT decreased association with 30S ribosomal subunit in vitro.
FT Grows slowly, cells have abnormal morphology."
FT /evidence="ECO:0000269|PubMed:22544754"
FT MUTAGEN 166
FT /note="T->D: Higher endogenous GTPase activity, GTPase more
FT stimulated by 70S ribosomes than wild-type, increased
FT association with 30S ribosomal subunit in vitro, wild-type
FT behavior in vivo."
FT /evidence="ECO:0000269|PubMed:22544754"
FT MUTAGEN 177
FT /note="K->A: Grows slowly, cells have abnormal morphology."
FT /evidence="ECO:0000269|PubMed:22544754"
FT MUTAGEN 178
FT /note="S->A: No GTPase activity. Wild-type phosphorylation
FT by PrkC in vitro."
FT /evidence="ECO:0000269|PubMed:16485133"
FT MUTAGEN 192
FT /note="T->A: Loss of phosphorylation by PrkC, but PrkC
FT autophosphorylation greatly decreased in vitro."
FT /evidence="ECO:0000269|PubMed:19246764"
FT MUTAGEN 196
FT /note="S->A: Wild-type phosphorylation by PrkC in vitro."
FT /evidence="ECO:0000269|PubMed:19246764"
FT MUTAGEN 206
FT /note="T->A: Wild-type phosphorylation by PrkC in vitro."
FT /evidence="ECO:0000269|PubMed:19246764"
FT MUTAGEN 222
FT /note="T->A: Wild-type phosphorylation by PrkC in vitro."
FT /evidence="ECO:0000269|PubMed:19246764"
FT MUTAGEN 226
FT /note="S->A: Loss of phosphorylation by PrkC, but PrkC
FT autophosphorylation considerably decreased in vitro."
FT /evidence="ECO:0000269|PubMed:19246764"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1T9H"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1T9H"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:1T9H"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1T9H"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1T9H"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:1T9H"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:1T9H"
SQ SEQUENCE 298 AA; 33797 MW; E58A69CAE570F855 CRC64;
MPEGKIIKAL SGFYYVLDES EDSDKVIQCR GRGIFRKNKI TPLVGDYVVY QAENDKEGYL
MEIKERTNEL IRPPICNVDQ AVLVFSAVQP SFSTALLDRF LVLVEANDIQ PIICITKMDL
IEDQDTEDTI QAYAEDYRNI GYDVYLTSSK DQDSLADIIP HFQDKTTVFA GQSGVGKSSL
LNAISPELGL RTNEISEHLG RGKHTTRHVE LIHTSGGLVA DTPGFSSLEF TDIEEEELGY
TFPDIREKSS SCKFRGCLHL KEPKCAVKQA VEDGELKQYR YDHYVEFMTE IKDRKPRY
