P06628 (SP0F_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sporulation initiation phosphotransferase F
EC=2.7.-.-

Alternative name(s):
Stage 0 sporulation protein F

Gene names

Name:	spo0F
Ordered Locus Names:	BSU37130

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

General annotation (Comments)

Function	Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
Cofactor	Binds 1 magnesium ion per subunit.
Subcellular location	Cytoplasm Probable.
Post-translational modification	Phosphorylated by KinA and KinB. Dephosphorylated by RapA and RapB.
Sequence similarities	Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Sporulation Two-component regulatory system
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
kinA	P16497	2	EBI-6418009,EBI-6405707

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 124

124

Sporulation initiation phosphotransferase F

PRO_0000081244

Regions

Domain

1 – 119

119

Response regulatory

Sites

Metal binding

10

1

Magnesium

Metal binding

11

1

Magnesium

Metal binding

54

1

Magnesium

Metal binding

56

1

Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue

54

1

4-aspartylphosphate

Secondary structure

1

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124

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

13 – 24

12

Turn

25 – 27

3

Beta strand

29 – 35

7

Helix

36 – 46

11

Beta strand

49 – 55

7

Beta strand

58 – 60

3

Helix

62 – 72

11

Beta strand

77 – 84

8

Helix

87 – 96

10

Beta strand

101 – 105

5

Helix

108 – 118

11

Beta strand

122 – 124

3

Sequences

	Sequence		Length	Mass (Da)
	P06628 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 4130377E3558D698	FASTA	124	14,228
	10 20 30 40 50 60 MMNEKILIVD DQYGIRILLN EVFNKEGYQT FQAANGLQAL DIVTKERPDL VLLDMKIPGM 70 80 90 100 110 120 DGIEILKRMK VIDENIRVII MTAYGELDMI QESKELGALT HFAKPFDIDE IRDAVKKYLP LKSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Revised assignment for the Bacillus subtilis spo0F gene and its homology with spo0A and with two Escherichia coli genes." Yoshikawa H., Kazami J., Yamashita S., Chibazakura T., Sone H., Kawamura F., Oda M., Isaka M., Kobayashi Y., Saito H. Nucleic Acids Res. 14:1063-1072(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins." Trach K.A., Chapman J.W., Piggot P.J., Hoch J.A. Proc. Natl. Acad. Sci. U.S.A. 82:7260-7264(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[3]	"Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome." Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A. J. Bacteriol. 170:4194-4208(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[4]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[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]	"1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR." Feher V.A., Zapf J.W., Hoch J.A., Dahlquist F.W., Whiteley J.M., Cavanagh J. Protein Sci. 4:1801-1814(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[7]	"High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition." Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntosh L.P., Rance M., Skelton N.J., Dahlquist F.W., Cavanagh J. Biochemistry 36:10015-10025(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[8]	"Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis." Madhusudan X., Zapf J., Whiteley J.M., Hoch J.A., Xuong N.H., Varughese K.I. Structure 4:679-690(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-13.
[9]	"A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis." Madhusudan X., Zapf J., Hoch J.A., Whiteley J.M., Xuong N.H., Varughese K.I. Biochemistry 36:12739-12745(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[10]	"A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction." Zapf J., Sen U., Madhusudan X., Hoch J.A., Varughese K.I. Structure 8:851-862(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03497 Genomic DNA. Translation: CAA27217.1.
M11081 Genomic DNA. Translation: AAA22787.1.
M22039 Unassigned DNA. Translation: AAA16802.1.
Z49782 Genomic DNA. Translation: CAA89872.1.
AL009126 Genomic DNA. Translation: CAB15730.1.

PIR

SZBS0F. A24737.

RefSeq

NP_391594.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F51	X-ray	3.00	E/F/G/H	3-121	[»]
1FSP	NMR	-	A	1-124	[»]
1NAT	X-ray	2.45	A	1-124	[»]
1PEY	X-ray	2.25	A/B/C	1-124	[»]
1PUX	NMR	-	A	1-124	[»]
1SRR	X-ray	1.90	A/B/C	1-124	[»]
2FSP	NMR	-	A	1-124	[»]
2FTK	X-ray	3.05	E/F/G/H	1-124	[»]
2JVI	NMR	-	A	1-124	[»]
2JVJ	NMR	-	A	1-124	[»]
2JVK	NMR	-	A	1-124	[»]
3Q15	X-ray	2.19	C/D	1-124	[»]

ProteinModelPortal

P06628.

SMR

P06628. Positions 4-119.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-58965N.

IntAct

P06628. 3 interactions.

STRING

224308.BSU37130.

Proteomic databases

PaxDb

P06628.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15730; CAB15730; BSU37130.

GeneID

937041.

KEGG

bsu:BSU37130.

PATRIC

18979462. VBIBacSub10457_3893.

Organism-specific databases

GenoList

BSU37130. [Micado]

Phylogenomic databases

eggNOG

COG0784.

HOGENOM

HOG000034820.

KO

K02490.

OMA

IRVIIMT.

ProtClustDB

CLSK873695.

Enzyme and pathway databases

BioCyc

BSUB:BSU37130-MONOMER.

Family and domain databases

InterPro

IPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Pfam

PF00072. Response_reg. 1 hit.
[Graphical view]

SMART

SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF52172. CheY_like. 1 hit.

PROSITE

PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06628.

ChEMBL

CHEMBL3857.

EvolutionaryTrace

P06628.

Entry information

Entry name

SP0F_BACSU

Accession

Primary (citable) accession number: P06628

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program