P39583 (YWAC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTP pyrophosphokinase YwaC
EC=2.7.6.5

Alternative name(s):
(p)ppGpp synthase YwaC
Small alarmone synthase 2
Short name=SAS 2

Gene names

Name:	ywaC
Ordered Locus Names:	BSU38480
ORF Names:	ipa-7d

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as a (p)ppGpp synthase. In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. activities in response to changes in nutritional abundance. YwaC has probably a minor role in stringent response. Ref.3
Catalytic activity	ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
Pathway	Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
Induction	Expressed during exponential growth with a marked and transient increase at the onset of the stationary phase. Induced by alkaline shock. Ref.3
Miscellaneous	GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis. The synthase activity of YwaC is weaker than that of YjbM.
Sequence similarities	Belongs to the RelA/SpoT family.

Ontologies

Keywords
Ligand	ATP-binding GTP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	guanosine tetraphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP diphosphokinase activity Inferred from electronic annotation. Source: EC kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 210	210	GTP pyrophosphokinase YwaC		PRO_0000049949

Sequences

	Sequence		Length	Mass (Da)
	P39583 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 6F981DF0D31A14FC	FASTA	210	24,600
	10 20 30 40 50 60 MDLSVTHMDD LKTVMEDWKN ELLVYKFALD ALDTKFSIIS QEYNLIHGHN PIEHTKSRVK 70 80 90 100 110 120 SFESIVNKLM RKGCEITTKE MKEHIHDIAG VRIICSFISD IYNVVNVLKQ HEDLRIVKVK 130 140 150 160 170 180 DYIQTPKPNG YRSLHLIIEM PVNLTNRVEY VKAEIQIRTI AMDFWASLEH KIYYKLNNDV 190 200 210 PKQLTDELKE AAEIAHYLDE KMLGIKKEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees." Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A. Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Identification and functional analysis of novel (p)ppGpp synthetase genes in Bacillus subtilis." Nanamiya H., Kasai K., Nozawa A., Yun C.S., Narisawa T., Murakami K., Natori Y., Kawamura F., Tozawa Y. Mol. Microbiol. 67:291-304(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A (P)PPGPP SYNTHASE, INDUCTION. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73124 Genomic DNA. Translation: CAA51563.1. AL009126 Genomic DNA. Translation: CAB15874.1.
PIR	S39662.
RefSeq	NP_391727.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P39583.
SMR	P39583. Positions 16-210.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39583. 1 interaction.
STRING	224308.BSU38480.
Proteomic databases
PaxDb	P39583.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB15874; CAB15874; BSU38480.
GeneID	937355.
KEGG	bsu:BSU38480.
PATRIC	18979742. VBIBacSub10457_4033.
Organism-specific databases
GenoList	BSU38480.
Phylogenomic databases
eggNOG	COG2357.
HOGENOM	HOG000263234.
OMA	ITCSFIA.
ProtClustDB	CLSK2502636.
Enzyme and pathway databases
BioCyc	BSUB:BSU38480-MONOMER.
UniPathway	UPA00908; UER00884.
Family and domain databases
InterPro	IPR026020. (p)ppGpp_Synthase. IPR007685. RelA_SpoT. [Graphical view]
PANTHER	PTHR21262. PTHR21262. 1 hit.
Pfam	PF04607. RelA_SpoT. 1 hit. [Graphical view]
SMART	SM00954. RelA_SpoT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YWAC_BACSU

Accession

Primary (citable) accession number: P39583

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program