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Protein

Histidine kinase 5

Gene

AHK5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Negative regulator of the ETR1-dependent abscisic acid (ABA) and ethylene signaling pathway that inhibits the root elongation. Promotes stomatal closure. Regulates stomatal opening by integrating multiple signals via hydrogen peroxide H2O2 homeostasis in guard cells in an ABA-independent manner. May contribute to basal defense mechanisms by closing stomata in the presence of bacterial pathogens. Regulates both hormone levels and ROS production in response to stress. Required for full immunity to bacterial pathogen and necrotrophic fungus.5 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi785 – 7851Magnesium
Metal bindingi828 – 8281Magnesium
Metal bindingi830 – 8301Magnesium; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB-KW
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to molecule of bacterial origin Source: UniProtKB
  • cellular response to nitric oxide Source: UniProtKB
  • cytokinin-activated signaling pathway Source: TAIR
  • defense response Source: UniProtKB-KW
  • ethylene-activated signaling pathway Source: UniProtKB-KW
  • negative regulation of abscisic acid-activated signaling pathway Source: UniProtKB
  • negative regulation of ethylene-activated signaling pathway Source: UniProtKB
  • peptidyl-histidine phosphorylation Source: GOC
  • regulation of stomatal closure Source: UniProtKB
  • root development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase

Keywords - Biological processi

Abscisic acid signaling pathway, Ethylene signaling pathway, Plant defense

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT5G10720-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine kinase 5 (EC:2.7.13.3)
Alternative name(s):
Arabidopsis histidine kinase 5
Short name:
AtHK5
Protein AUTHENTIC HIS-KINASE 5
Protein CYTOKININ-INDEPENDENT 2
Gene namesi
Name:AHK5
Synonyms:CKI2
Ordered Locus Names:At5g10720
ORF Names:MAJ23.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G10720.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Hypersensitive to abscisic acid (ABA) and ethylene (ACC) in roots. Reduced stomatal closure in response to H2O2, bacterial pathogen associated molecular pattern (PAMP) flagellin, Pseudomonas syringae, darkness, nitric oxide and ethylene, but normal closure in response to ABA and the peptide elf. Increased sensitivity to pathogens and increased tolerance to high salinity.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 922922Histidine kinase 5PRO_0000398590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei376 – 3761Phosphohistidine; by autocatalysisPROSITE-ProRule annotation
Modified residuei828 – 82814-aspartylphosphateCurated

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3S4A7.
PRIDEiQ3S4A7.

Expressioni

Tissue specificityi

Present in light-grown but not in etiolated seedlings. Mostly expressed in roots flowers and siliques, and, to a lower extent, in stems and leaves, especially in guard cells.2 Publications

Inductioni

By H2O2.1 Publication

Gene expression databases

GenevisibleiQ3S4A7. AT.

Interactioni

Subunit structurei

Interacts with AHP1, APH2, APH3, APH5 and APH6, but not with APH4.1 Publication

Protein-protein interaction databases

BioGridi16216. 6 interactions.
STRINGi3702.AT5G10720.1.

Structurei

Secondary structure

1
922
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi780 – 7834Combined sources
Helixi787 – 79913Combined sources
Beta strandi805 – 8095Combined sources
Helixi810 – 81910Combined sources
Beta strandi823 – 8308Combined sources
Beta strandi832 – 8343Combined sources
Helixi836 – 84914Combined sources
Helixi853 – 8575Combined sources
Beta strandi880 – 8845Combined sources
Helixi888 – 8903Combined sources
Helixi892 – 8976Combined sources
Beta strandi901 – 9077Combined sources
Helixi910 – 92011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EUKX-ray1.95A774-922[»]
ProteinModelPortaliQ3S4A7.
SMRiQ3S4A7. Positions 320-613, 776-922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini373 – 614242Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini779 – 921143Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili86 – 12035Sequence analysisAdd
BLAST
Coiled coili169 – 20537Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IRDD. Eukaryota.
ENOG410XNMH. LUCA.
HOGENOMiHOG000241999.
InParanoidiQ3S4A7.
OMAiFGEHHEG.
PhylomeDBiQ3S4A7.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3S4A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVCEMETDQI EEMDVEVLSS MWPEDVGTEA DKQFNVEKPA GDLDTLKEVT
60 70 80 90 100
IETRTIADMT RLPNLLNSTH QGSSQLTNLV KQWEYMQDNA VRLLKEELKN
110 120 130 140 150
LDRQREEAEA KELKIIEEYK FESNEPENVP VLDETSDLFR RFRQKKRDAL
160 170 180 190 200
VDSKKIEIYE EFDTVAYWKQ KALSLEKMLE ASTERERRLM EKLSESLKTM
210 220 230 240 250
ESQSAPVQEL TQNLKRAEGF LHFILQNAPI VMGHQDKDLR YLFIYNKYPS
260 270 280 290 300
LREQDILGKT DVEIFHGGGV KESEDFKREV LEKGKASKRE ITFTTDLFGS
310 320 330 340 350
KTFLIYVEPV YNKAGEKIGI NYMGMEVTDQ VVKREKMAKL REDNAVRKAM
360 370 380 390 400
ESELNKTIHI TEETMRAKQM LATMSHEIRS PLSGVVGMAE ILSTTKLDKE
410 420 430 440 450
QRQLLNVMIS SGDLVLQLIN DILDLSKVES GVMRLEATKF RPREVVKHVL
460 470 480 490 500
QTAAASLKKS LTLEGNIADD VPIEVVGDVL RIRQILTNLI SNAIKFTHEG
510 520 530 540 550
NVGIKLQVIS EPSFVRDNAL NADTEEHEQN GLTETSVWIC CDVWDTGIGI
560 570 580 590 600
PENALPCLFK KYMQASADHA RKYGGTGLGL AICKQLVELM GGQLTVTSRV
610 620 630 640 650
SEGSTFTFIL PYKVGRSDDY SDDQDEFSDM ADQQSEPDDT AEGYFQFKPL
660 670 680 690 700
LGSIYSNGGP GISNDFLPHK VMLTSPIKLI NGFVADPSNN TGQSEMLQLE
710 720 730 740 750
NGGYMDESKL ETSSGHCPES AHQYENGNGR CFSKESESCS SSQASSEGGT
760 770 780 790 800
LEMESELTVS SHREEEKAET EVKETSKPKI LLVEDNKINI MVAKSMMKQL
810 820 830 840 850
GHTMDIANNG VEAITAINSS SYDLVLMDVC MPVLDGLKAT RLIRSYEETG
860 870 880 890 900
NWNAAIEAGV DISTSENEQV CMRPTNRLPI IAMTANTLAE SSEECYANGM
910 920
DSFISKPVTL QKLRECLQQY LH
Length:922
Mass (Da):103,637
Last modified:October 11, 2005 - v1
Checksum:i3E5CA8DD7C18DD16
GO

Sequence cautioni

The sequence CAC08246.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ167579 mRNA. Translation: AAZ98829.1.
AL392144 Genomic DNA. Translation: CAC08246.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91588.1.
RefSeqiNP_196633.2. NM_121110.2.
UniGeneiAt.19135.
At.54804.

Genome annotation databases

EnsemblPlantsiAT5G10720.1; AT5G10720.1; AT5G10720.
GeneIDi830938.
GrameneiAT5G10720.1; AT5G10720.1; AT5G10720.
KEGGiath:AT5G10720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ167579 mRNA. Translation: AAZ98829.1.
AL392144 Genomic DNA. Translation: CAC08246.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91588.1.
RefSeqiNP_196633.2. NM_121110.2.
UniGeneiAt.19135.
At.54804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EUKX-ray1.95A774-922[»]
ProteinModelPortaliQ3S4A7.
SMRiQ3S4A7. Positions 320-613, 776-922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16216. 6 interactions.
STRINGi3702.AT5G10720.1.

Proteomic databases

PaxDbiQ3S4A7.
PRIDEiQ3S4A7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G10720.1; AT5G10720.1; AT5G10720.
GeneIDi830938.
GrameneiAT5G10720.1; AT5G10720.1; AT5G10720.
KEGGiath:AT5G10720.

Organism-specific databases

TAIRiAT5G10720.

Phylogenomic databases

eggNOGiENOG410IRDD. Eukaryota.
ENOG410XNMH. LUCA.
HOGENOMiHOG000241999.
InParanoidiQ3S4A7.
OMAiFGEHHEG.
PhylomeDBiQ3S4A7.

Enzyme and pathway databases

BioCyciARA:AT5G10720-MONOMER.

Miscellaneous databases

PROiQ3S4A7.

Gene expression databases

GenevisibleiQ3S4A7. AT.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cytokinin independent 2 is an intracellular histidine kinase modulating cytokinin-dependent growth."
    Meister R.J., Sivasankar S.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "AHK5 histidine kinase regulates root elongation through an ETR1-dependent abscisic acid and ethylene signaling pathway in Arabidopsis thaliana."
    Iwama A., Yamashino T., Tanaka Y., Sakakibara H., Kakimoto T., Sato S., Kato T., Tabata S., Nagatani A., Mizuno T.
    Plant Cell Physiol. 48:375-380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  5. "Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases in response to abscisic acid, drought, and salt stress in Arabidopsis."
    Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K., Yamaguchi-Shinozaki K.
    Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The histidine kinase AHK5 integrates endogenous and environmental signals in Arabidopsis guard cells."
    Desikan R., Horak J., Chaban C., Mira-Rodado V., Witthoeft J., Elgass K., Grefen C., Cheung M.-K., Meixner A.J., Hooley R., Neill S.J., Hancock J.T., Harter K.
    PLoS ONE 3:E2491-E2491(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION BY HYDROGEN PEROXIDE.
  7. "Arabidopsis histidine kinase 5 regulates salt sensitivity and resistance against bacterial and fungal infection."
    Pham J., Liu J., Bennett M.H., Mansfield J.W., Desikan R.
    New Phytol. 194:168-180(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Modulation of ROS production and hormone levels by AHK5 during abiotic and biotic stress signaling."
    Pham J., Desikan R.
    Plant Signal. Behav. 7:893-897(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Structure-function analysis of Arabidopsis thaliana histidine kinase AHK5 bound to its cognate phosphotransfer protein AHP1."
    Bauer J., Reiss K., Veerabagu M., Heunemann M., Harter K., Stehle T.
    Mol. Plant 6:959-970(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH AHP1, INTERACTION WITH AHP1; APH2; APH3; APH5 AND APH6.

Entry informationi

Entry nameiAHK5_ARATH
AccessioniPrimary (citable) accession number: Q3S4A7
Secondary accession number(s): Q9FT60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.