P06534 (SP0A_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Stage 0 sporulation protein A

Alternative name(s):
Stage 0 sporulation protein C
Stage 0 sporulation protein G

Gene names

Name:	spo0A
Synonyms:	spo0C, spo0G
Ordered Locus Names:	BSU24220

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	267 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box).
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Cytoplasm Probable.
Post-translational modification	Phosphorylated by KinA and KinB.
Miscellaneous	Stage 0 mutants lack the ability to form the asymmetric septum characteristic of the initiation of the sporulation process.
Sequence similarities	Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Sporulation Transcription Transcription regulation Two-component regulatory system
Cellular component	Cytoplasm
Ligand	Calcium DNA-binding Metal-binding
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	asymmetric cell division Inferred from genetic interaction PubMed 18573177. Source: UniProtKB barrier septum assembly Inferred from genetic interaction PubMed 18573177. Source: UniProtKB detection of stimulus involved in sensory perception Inferred from electronic annotation. Source: InterPro intracellular signal transduction Inferred from electronic annotation. Source: GOC positive regulation of sporulation resulting in formation of a cellular spore Inferred from genetic interaction PubMed 18573177. Source: UniProtKB sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: InterPro phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Stage 0 sporulation protein A

PRO_0000081234

Regions

Domain

1 – 123

123

Response regulatory

DNA binding

199 – 218

20

H-T-H motif Potential

Sites

Metal binding

10

1

Calcium By similarity

Metal binding

11

1

Calcium By similarity

Metal binding

56

1

Calcium By similarity

Amino acid modifications

Modified residue

56

1

4-aspartylphosphate By similarity

Experimental info

Mutagenesis

12

1

N → S in SOF-1 mutant. Ref.8

Mutagenesis

60

1

P → S in COI-1 mutant. Ref.8

Mutagenesis

87

1

A → V in COI-2 and COI-12 mutants. Ref.8

Mutagenesis

90

1

Q → K in COI-15 mutant. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

267

Helix Strand Turn

Details...

Helix

153 – 164

12

Helix

171 – 185

15

Helix

187 – 191

5

Turn

193 – 196

4

Helix

197 – 204

8

Helix

209 – 225

17

Helix

231 – 235

5

Helix

249 – 262

14

Sequences

	Sequence		Length	Mass (Da)
	P06534 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 2F4943A5A5061DD9	FASTA	267	29,691
	10 20 30 40 50 60 MEKIKVCVAD DNRELVSLLS EYIEGQEDME VIGVAYNGQE CLSLFKEKDP DVLVLDIIMP 70 80 90 100 110 120 HLDGLAVLER LRESDLKKQP NVIMLTAFGQ EDVTKKAVDL GASYFILKPF DMENLVGHIR 130 140 150 160 170 180 QVSGNASSVT HRAPSSQSSI IRSSQPEPKK KNLDASITSI IHEIGVPAHI KGYLYLREAI 190 200 210 220 230 240 SMVYNDIELL GSITKVLYPD IAKKFNTTAS RVERAIRHAI EVAWSRGNID SISSLFGYTV 250 260 SMTKAKPTNS EFIAMVADKL RLEHKAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the sporulation gene spo0A and its mutant genes of Bacillus subtilis." Kudoh J., Ikeuchi T., Kurahashi K. Proc. Natl. Acad. Sci. U.S.A. 82:2665-2668(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Amino-terminal structure of spoOA protein and sequence homology with spoOF and spoOB proteins." Ikeuchi T., Kudoh J., Tsunasawa S. Mol. Gen. Genet. 203:371-376(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of the spo0A locus and its deduced product." Ferrari F.A., Trach K.A., Le Coq D., Spence J., Ferrari E., Hoch J.A. Proc. Natl. Acad. Sci. U.S.A. 82:2647-2651(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[5]	"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.
[6]	"SpoIVB has two distinct functions during spore formation in Bacillus subtilis." Oke V., Shchepetov M., Cutting S. Mol. Microbiol. 23:223-230(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. Strain: 168 / JH642.
[7]	"New suppressor mutation sur0B of spo0B and spo0F mutations in Bacillus subtilis." Shoji K., Hiratsuka S., Kawamura F., Kobayashi Y. J. Gen. Microbiol. 134:3249-3257(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[8]	"Novel mutations that alter the regulation of sporulation in Bacillus subtilis. Evidence that phosphorylation of regulatory protein SpoOA controls the initiation of sporulation." Olmedo G., Gottlin Ninfa E., Stock J., Youngman P. J. Mol. Biol. 215:359-372(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-12; PRO-60; ALA-87 AND GLN-90.
[9]	"DNA complexed structure of the key transcription factor initiating development in sporulating bacteria." Zhao H., Msadek T., Zapf J., Madhusudan X., Hoch J.A., Varughese K.I. Structure 10:1041-1050(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 148-267.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M10082 Genomic DNA. Translation: AAA22786.1.
D84432 Genomic DNA. Translation: BAA12581.1.
AL009126 Genomic DNA. Translation: CAB14353.1.
U68235 Genomic DNA. Translation: AAC44872.1.
M23656 Genomic DNA. Translation: AAA22842.1.

PIR

SZBS0A. A94036.

RefSeq

NP_390302.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LQ1	X-ray	2.30	A/B/C/D	148-267	[»]

ProteinModelPortal

P06534.

SMR

P06534. Positions 4-124, 151-266.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU24220.

Proteomic databases

PaxDb

P06534.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14353; CAB14353; BSU24220.

GeneID

938655.

KEGG

bsu:BSU24220.

PATRIC

18976676. VBIBacSub10457_2528.

Organism-specific databases

GenoList

BSU24220. [Micado]

Phylogenomic databases

eggNOG

COG0784.

HOGENOM

HOG000057639.

KO

K07699.

OMA

RGKPTNS.

ProtClustDB

CLSK873420.

Enzyme and pathway databases

BioCyc

BSUB:BSU24220-MONOMER.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR011006. CheY-like_superfamily.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR014879. Spo0A_C.
IPR012052. Spore_0_A.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00072. Response_reg. 1 hit.
PF08769. Spo0A_C. 1 hit.
[Graphical view]

PIRSF

PIRSF002937. Res_reg_Spo0A. 1 hit.

ProDom

PD010908. Spo0A_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF46894. Bipartite_resp_reg_C-effector. 1 hit.
SSF52172. CheY_like. 1 hit.

TIGRFAMs

TIGR02875. spore_0_A. 1 hit.

PROSITE

PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06534.

Entry information

Entry name

SP0A_BACSU

Accession

Primary (citable) accession number: P06534
Secondary accession number(s): P70990

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program