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Protein

Sporulation kinase A

Gene

kinA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. phosphorelay sensor kinase activity Source: GO_Central

GO - Biological processi

  1. peptidyl-histidine phosphorylation Source: GO_Central
  2. phosphorelay signal transduction system Source: GO_Central
  3. positive regulation of sporulation Source: CACAO
  4. regulation of transcription, DNA-templated Source: InterPro
  5. signal transduction by phosphorylation Source: GOC
  6. sporulation resulting in formation of a cellular spore Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Sporulation, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU13990-MONOMER.
BRENDAi2.7.13.3. 700.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation kinase A (EC:2.7.13.3)
Alternative name(s):
Stage II sporulation protein F
Stage II sporulation protein J
Gene namesi
Name:kinA
Synonyms:gsiC, scoD, spoIIF, spoIIJ
Ordered Locus Names:BSU13990
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU13990. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 606606Sporulation kinase APRO_0000074776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP16497.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-6405707,EBI-6405707
sdaQ7WY626EBI-6405707,EBI-6405714
spo0FP066282EBI-6405707,EBI-6418009

Protein-protein interaction databases

DIPiDIP-58966N.
IntActiP16497. 2 interactions.
STRINGi224308.BSU13990.

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215Combined sources
Beta strandi25 – 306Combined sources
Helixi34 – 385Combined sources
Helixi42 – 454Combined sources
Helixi50 – 534Combined sources
Helixi56 – 583Combined sources
Helixi59 – 679Combined sources
Beta strandi75 – 806Combined sources
Beta strandi86 – 9510Combined sources
Beta strandi107 – 1137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VLGX-ray1.70A/B/C/D10-117[»]
ProteinModelPortaliP16497.
SMRiP16497. Positions 15-116, 374-606.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7371PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 11640PAC 1Add
BLAST
Domaini140 – 21475PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini218 – 25538PAC 2Add
BLAST
Domaini265 – 33571PAS 3PROSITE-ProRule annotationAdd
BLAST
Domaini402 – 606205Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 3 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000008904.
InParanoidiP16497.
KOiK02491.
OMAiLMVTFNI.
OrthoDBiEOG69GZGV.
PhylomeDBiP16497.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_C.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 2 hits.
SM00091. PAS. 3 hits.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF55785. SSF55785. 3 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 3 hits.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16497-1 [UniParc]FASTAAdd to Basket

« Hide

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

ISFPKK
Length:606
Mass (Da):69,171
Last modified:July 15, 1998 - v2
Checksum:iA8BB97FE844B32EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761S → F in AAA22800. (PubMed:2104615)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29450 Genomic DNA. Translation: AAA22800.1.
M31067 Genomic DNA. Translation: AAA22664.1.
AJ222587 Genomic DNA. Translation: CAA10862.1.
AL009126 Genomic DNA. Translation: CAB13272.1.
PIRiA33496.
RefSeqiNP_389282.1. NC_000964.3.
WP_003245779.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13272; CAB13272; BSU13990.
GeneIDi939230.
KEGGibsu:BSU13990.
PATRICi18974581. VBIBacSub10457_1482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29450 Genomic DNA. Translation: AAA22800.1.
M31067 Genomic DNA. Translation: AAA22664.1.
AJ222587 Genomic DNA. Translation: CAA10862.1.
AL009126 Genomic DNA. Translation: CAB13272.1.
PIRiA33496.
RefSeqiNP_389282.1. NC_000964.3.
WP_003245779.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VLGX-ray1.70A/B/C/D10-117[»]
ProteinModelPortaliP16497.
SMRiP16497. Positions 15-116, 374-606.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58966N.
IntActiP16497. 2 interactions.
STRINGi224308.BSU13990.

Chemistry

ChEMBLiCHEMBL2111331.

Proteomic databases

PaxDbiP16497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13272; CAB13272; BSU13990.
GeneIDi939230.
KEGGibsu:BSU13990.
PATRICi18974581. VBIBacSub10457_1482.

Organism-specific databases

GenoListiBSU13990. [Micado]

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000008904.
InParanoidiP16497.
KOiK02491.
OMAiLMVTFNI.
OrthoDBiEOG69GZGV.
PhylomeDBiP16497.

Enzyme and pathway databases

BioCyciBSUB:BSU13990-MONOMER.
BRENDAi2.7.13.3. 700.

Miscellaneous databases

EvolutionaryTraceiP16497.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_C.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 2 hits.
SM00091. PAS. 3 hits.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF55785. SSF55785. 3 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 3 hits.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiKINA_BACSU
AccessioniPrimary (citable) accession number: P16497
Secondary accession number(s): P22863
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 15, 1998
Last modified: February 4, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.