YWAC_BACSU
ID YWAC_BACSU Reviewed; 210 AA.
AC P39583;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=GTP pyrophosphokinase YwaC;
DE EC=2.7.6.5;
DE AltName: Full=(p)ppGpp synthase YwaC;
DE AltName: Full=Small alarmone synthase 2 {ECO:0000303|PubMed:18067544};
DE Short=SAS 2 {ECO:0000303|PubMed:18067544};
GN Name=ywaC; OrderedLocusNames=BSU38480; ORFNames=ipa-7d;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
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 FUNCTION AS A (P)PPGPP SYNTHASE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=18067544; DOI=10.1111/j.1365-2958.2007.06018.x;
RA Nanamiya H., Kasai K., Nozawa A., Yun C.S., Narisawa T., Murakami K.,
RA Natori Y., Kawamura F., Tozawa Y.;
RT "Identification and functional analysis of novel (p)ppGpp synthetase genes
RT in Bacillus subtilis.";
RL Mol. Microbiol. 67:291-304(2008).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ASP-87 AND LEU-176.
RC STRAIN=168;
RX PubMed=22950019; DOI=10.1002/mbo3.16;
RA Tagami K., Nanamiya H., Kazo Y., Maehashi M., Suzuki S., Namba E.,
RA Hoshiya M., Hanai R., Tozawa Y., Morimoto T., Ogasawara N., Kageyama Y.,
RA Ara K., Ozaki K., Yoshida M., Kuroiwa H., Kuroiwa T., Ohashi Y.,
RA Kawamura F.;
RT "Expression of a small (p)ppGpp synthetase, YwaC, in the (p)ppGpp(0) mutant
RT of Bacillus subtilis triggers YvyD-dependent dimerization of ribosome.";
RL MicrobiologyOpen 1:115-134(2012).
CC -!- FUNCTION: Functions as a (p)ppGpp synthase; GDP can be used instead of
CC GTP, resulting in an increase of (p)ppGpp synthesis (PubMed:18067544).
CC Overexpression in relA mutants (triple relA-yjbM-ywaC deletions and
CC single relA deletions) leads to growth arrest; GTP levels fall
CC drastically, various guanine-related nucleotides are synthesized (ppGp
CC or pGpp), the cellular transcriptional profile changes dramatically and
CC 70S ribosome dimerization occurs (PubMed:22950019). Overexpression in
CC the presence of a wild-type relA gene does not have these effects
CC (PubMed:22950019). In eubacteria ppGpp (guanosine 3'-diphosphate 5'-
CC diphosphate) is a mediator of the stringent response that coordinates a
CC variety of cellular activities in response to changes in nutritional
CC abundance. activities in response to changes in nutritional abundance.
CC YwaC has probably a minor role in stringent response (PubMed:18067544).
CC {ECO:0000269|PubMed:18067544, ECO:0000269|PubMed:22950019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O31611}.
CC -!- INDUCTION: Weakly expressed during exponential growth with a marked and
CC transient increase at the onset of the stationary phase
CC (PubMed:18067544). Protein expression is very low during the first 3.5
CC hours after inoculation (at protein level) (PubMed:22950019). Induced
CC by alkaline shock (PubMed:18067544). {ECO:0000269|PubMed:18067544,
CC ECO:0000269|PubMed:22950019}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, double yjbM-ywaC and triple
CC relA-yjbM-ywaC mutants are also viable (PubMed:18067544).
CC {ECO:0000269|PubMed:18067544}.
CC -!- MISCELLANEOUS: The synthase activity of YwaC is weaker than that of
CC YjbM (PubMed:18067544). {ECO:0000269|PubMed:18067544}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; X73124; CAA51563.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15874.1; -; Genomic_DNA.
DR PIR; S39662; S39662.
DR RefSeq; NP_391727.1; NC_000964.3.
DR RefSeq; WP_003244564.1; NZ_JNCM01000034.1.
DR PDB; 6FGK; X-ray; 3.20 A; A/B/C/D=1-210.
DR PDBsum; 6FGK; -.
DR AlphaFoldDB; P39583; -.
DR SMR; P39583; -.
DR IntAct; P39583; 1.
DR STRING; 224308.BSU38480; -.
DR PaxDb; P39583; -.
DR PRIDE; P39583; -.
DR EnsemblBacteria; CAB15874; CAB15874; BSU_38480.
DR GeneID; 937355; -.
DR KEGG; bsu:BSU38480; -.
DR PATRIC; fig|224308.179.peg.4165; -.
DR eggNOG; COG2357; Bacteria.
DR InParanoid; P39583; -.
DR OMA; GLRITCS; -.
DR PhylomeDB; P39583; -.
DR BioCyc; BSUB:BSU38480-MON; -.
DR BRENDA; 2.7.6.5; 658.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; GTP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="GTP pyrophosphokinase YwaC"
FT /id="PRO_0000049949"
FT MUTAGEN 87
FT /note="D->G: No longer inhibits growth when overexpressed
FT in relA mutants, probably does not synthesisize (p)ppGpp.
FT 70S ribosomes no longer dimerize to form 100S ribosomes."
FT /evidence="ECO:0000269|PubMed:22950019"
FT MUTAGEN 176
FT /note="L->F: No longer inhibits growth when overexpressed
FT in relA mutants."
FT /evidence="ECO:0000269|PubMed:22950019"
FT HELIX 18..41
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:6FGK"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:6FGK"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:6FGK"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:6FGK"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:6FGK"
FT HELIX 182..207
FT /evidence="ECO:0007829|PDB:6FGK"
SQ SEQUENCE 210 AA; 24600 MW; 6F981DF0D31A14FC CRC64;
MDLSVTHMDD LKTVMEDWKN ELLVYKFALD ALDTKFSIIS QEYNLIHGHN PIEHTKSRVK
SFESIVNKLM RKGCEITTKE MKEHIHDIAG VRIICSFISD IYNVVNVLKQ HEDLRIVKVK
DYIQTPKPNG YRSLHLIIEM PVNLTNRVEY VKAEIQIRTI AMDFWASLEH KIYYKLNNDV
PKQLTDELKE AAEIAHYLDE KMLGIKKEVD
