P16497 (KINA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sporulation kinase A
EC=2.7.13.3

Alternative name(s):
Stage II sporulation protein F
Stage II sporulation protein J

Gene names

Name:	kinA
Synonyms:	gsiC, scoD, spoIIF, spoIIJ
Ordered Locus Names:	BSU13990

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

General annotation (Comments)

Function	Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence similarities	Contains 1 histidine kinase domain. Contains 2 PAC (PAS-associated C-terminal) domains. Contains 3 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
Biological process	Sporulation Two-component regulatory system
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		8	EBI-6405707,EBI-6405707
sda	Q7WY62	6	EBI-6405707,EBI-6405714
spo0F	P06628	2	EBI-6405707,EBI-6418009

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 606

606

Sporulation kinase A

PRO_0000074776

Regions

Domain

3 – 73

71

PAS 1

Domain

77 – 116

40

PAC 1

Domain

140 – 214

75

PAS 2

Domain

218 – 255

38

PAC 2

Domain

265 – 335

71

PAS 3

Domain

402 – 606

205

Histidine kinase

Amino acid modifications

Modified residue

405

1

Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict

276

1

S → F in AAA22800. Ref.1

Secondary structure

1

.

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606

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Beta strand

25 – 30

6

Helix

34 – 38

5

Helix

42 – 45

4

Helix

50 – 53

4

Helix

56 – 58

3

Helix

59 – 67

9

Beta strand

75 – 80

6

Beta strand

86 – 95

10

Beta strand

107 – 113

7

Sequences

	Sequence		Length	Mass (Da)
	P16497 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: A8BB97FE844B32EE	FASTA	606	69,171
	10 20 30 40 50 60 MEQDTQHVKP LQTKTDIHAV LASNGRIIYI SANSKLHLGY LQGEMIGSFL KTFLHEEDQF 70 80 90 100 110 120 LVESYFYNEH HLMPCTFRFI KKDHTIVWVE AAVEIVTTRA ERTEREIILK MKVLEEETGH 130 140 150 160 170 180 QSLNCEKHEI EPASPESTTY ITDDYERLVE NLPSPLCISV KGKIVYVNSA MLSMLGAKSK 190 200 210 220 230 240 DAIIGKSSYE FIEEEYHDIV KNRIIRMQKG MEVGMIEQTW KRLDGTPVHL EVKASPTVYK 250 260 270 280 290 300 NQQAELLLLI DISSRKKFQT ILQKSRERYQ LLIQNSIDTI AVIHNGKWVF MNESGISLFE 310 320 330 340 350 360 AATYEDLIGK NIYDQLHPCD HEDVKERIQN IAEQKTESEI VKQSWFTFQN RVIYTEMVCI 370 380 390 400 410 420 PTTFFGEAAV QVILRDISER KQTEELMLKS EKLSIAGQLA AGIAHEIRNP LTAIKGFLQL 430 440 450 460 470 480 MKPTMEGNEH YFDIVFSELS RIELILSELL MLAKPQQNAV KEYLNLKKLI GEVSALLETQ 490 500 510 520 530 540 ANLNGIFIRT SYEKDSIYIN GDQNQLKQVF INLIKNAVES MPDGGTVDII ITEDEHSVHV 550 560 570 580 590 600 TVKDEGEGIP EKVLNRIGEP FLTTKEKGTG LGLMVTFNII ENHQGVIHVD SHPEKGTAFK ISFPKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The spoIIJ gene, which regulates early developmental steps in Bacillus subtilis, belongs to a class of environmentally responsive genes." Antoniewski C., Savelli B., Stragier P. J. Bacteriol. 172:86-93(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis." Perego M., Cole S.P., Burbulys D., Trach K., Hoch J.A. J. Bacteriol. 171:6187-6196(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"Sequence of the Bacillus subtilis chromosome from ykuA to cse-15." Scanlan E., Devine K.M. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29450 Genomic DNA. Translation: AAA22800.1.
M31067 Genomic DNA. Translation: AAA22664.1.
AJ222587 Genomic DNA. Translation: CAA10862.1.
AL009126 Genomic DNA. Translation: CAB13272.1.

PIR

A33496.

RefSeq

NP_389282.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VLG	X-ray	1.70	A/B/C/D	10-117	[»]

ProteinModelPortal

P16497.

SMR

P16497. Positions 15-116, 374-606.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-58966N.

IntAct

P16497. 2 interactions.

STRING

224308.BSU13990.

Proteomic databases

PaxDb

P16497.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13272; CAB13272; BSU13990.

GeneID

939230.

KEGG

bsu:BSU13990.

PATRIC

18974581. VBIBacSub10457_1482.

Organism-specific databases

GenoList

BSU13990. [Micado]

Phylogenomic databases

eggNOG

COG0642.

HOGENOM

HOG000008904.

KO

K02491.

OMA

TQANLNG.

ProtClustDB

CLSK887211.

Enzyme and pathway databases

BioCyc

BSUB:BSU13990-MONOMER.

BRENDA

2.7.13.3. 700.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR003594. HATPase_ATP-bd.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]

Pfam

PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 2 hits.
SM00091. PAS. 3 hits.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.

TIGRFAMs

TIGR00229. sensory_box. 3 hits.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50113. PAC. False negative.
PS50112. PAS. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16497.

ChEMBL

CHEMBL3889.

EvolutionaryTrace

P16497.

Entry information

Entry name

KINA_BACSU

Accession

Primary (citable) accession number: P16497
Secondary accession number(s): P22863

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program