AHK5_ARATH
ID AHK5_ARATH Reviewed; 922 AA.
AC Q3S4A7; Q9FT60;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Histidine kinase 5;
DE EC=2.7.13.3;
DE AltName: Full=Arabidopsis histidine kinase 5;
DE Short=AtHK5;
DE AltName: Full=Protein AUTHENTIC HIS-KINASE 5;
DE AltName: Full=Protein CYTOKININ-INDEPENDENT 2;
GN Name=AHK5; Synonyms=CKI2; OrderedLocusNames=At5g10720; ORFNames=MAJ23.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Meister R.J., Sivasankar S.;
RT "Cytokinin independent 2 is an intracellular histidine kinase modulating
RT cytokinin-dependent growth.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17202180; DOI=10.1093/pcp/pcl065;
RA Iwama A., Yamashino T., Tanaka Y., Sakakibara H., Kakimoto T., Sato S.,
RA Kato T., Tabata S., Nagatani A., Mizuno T.;
RT "AHK5 histidine kinase regulates root elongation through an ETR1-dependent
RT abscisic acid and ethylene signaling pathway in Arabidopsis thaliana.";
RL Plant Cell Physiol. 48:375-380(2007).
RN [5]
RP FUNCTION.
RX PubMed=18077346; DOI=10.1073/pnas.0706547105;
RA Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases
RT in response to abscisic acid, drought, and salt stress in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=18560512; DOI=10.1371/journal.pone.0002491;
RA Desikan R., Horak J., Chaban C., Mira-Rodado V., Witthoeft J., Elgass K.,
RA Grefen C., Cheung M.-K., Meixner A.J., Hooley R., Neill S.J., Hancock J.T.,
RA Harter K.;
RT "The histidine kinase AHK5 integrates endogenous and environmental signals
RT in Arabidopsis guard cells.";
RL PLoS ONE 3:E2491-E2491(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22256998; DOI=10.1111/j.1469-8137.2011.04033.x;
RA Pham J., Liu J., Bennett M.H., Mansfield J.W., Desikan R.;
RT "Arabidopsis histidine kinase 5 regulates salt sensitivity and resistance
RT against bacterial and fungal infection.";
RL New Phytol. 194:168-180(2012).
RN [8]
RP FUNCTION.
RX PubMed=22827948; DOI=10.4161/psb.20692;
RA Pham J., Desikan R.;
RT "Modulation of ROS production and hormone levels by AHK5 during abiotic and
RT biotic stress signaling.";
RL Plant Signal. Behav. 7:893-897(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH AHP1, AND
RP INTERACTION WITH AHP1; APH2; APH3; APH5 AND APH6.
RX PubMed=23132142; DOI=10.1093/mp/sss126;
RA Bauer J., Reiss K., Veerabagu M., Heunemann M., Harter K., Stehle T.;
RT "Structure-function analysis of Arabidopsis thaliana histidine kinase AHK5
RT bound to its cognate phosphotransfer protein AHP1.";
RL Mol. Plant 6:959-970(2013).
CC -!- FUNCTION: Functions as a histidine kinase and transmits the stress
CC signal to a downstream MAPK cascade. This protein undergoes an ATP-
CC dependent autophosphorylation at a conserved histidine residue in the
CC kinase core, and a phosphoryl group is then transferred to a conserved
CC aspartate residue in the receiver domain. Negative regulator of the
CC ETR1-dependent abscisic acid (ABA) and ethylene signaling pathway that
CC inhibits the root elongation. Promotes stomatal closure. Regulates
CC stomatal opening by integrating multiple signals via hydrogen peroxide
CC H(2)O(2) homeostasis in guard cells in an ABA-independent manner. May
CC contribute to basal defense mechanisms by closing stomata in the
CC presence of bacterial pathogens. Regulates both hormone levels and ROS
CC production in response to stress. Required for full immunity to
CC bacterial pathogen and necrotrophic fungus.
CC {ECO:0000269|PubMed:17202180, ECO:0000269|PubMed:18077346,
CC ECO:0000269|PubMed:18560512, ECO:0000269|PubMed:22256998,
CC ECO:0000269|PubMed:22827948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with AHP1, APH2, APH3, APH5 and APH6, but not with
CC APH4. {ECO:0000269|PubMed:23132142}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18560512};
CC Peripheral membrane protein {ECO:0000269|PubMed:18560512}. Cytoplasm
CC {ECO:0000269|PubMed:18560512}.
CC -!- TISSUE SPECIFICITY: Present in light-grown but not in etiolated
CC seedlings. Mostly expressed in roots flowers and siliques, and, to a
CC lower extent, in stems and leaves, especially in guard cells.
CC {ECO:0000269|PubMed:17202180, ECO:0000269|PubMed:18560512}.
CC -!- INDUCTION: By H(2)O(2). {ECO:0000269|PubMed:18560512}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to abscisic acid (ABA) and
CC ethylene (ACC) in roots. Reduced stomatal closure in response to
CC H(2)O(2), bacterial pathogen associated molecular pattern (PAMP)
CC flagellin, Pseudomonas syringae, darkness, nitric oxide and ethylene,
CC but normal closure in response to ABA and the peptide elf. Increased
CC sensitivity to pathogens and increased tolerance to high salinity.
CC {ECO:0000269|PubMed:17202180, ECO:0000269|PubMed:18560512,
CC ECO:0000269|PubMed:22256998}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC08246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ167579; AAZ98829.1; -; mRNA.
DR EMBL; AL392144; CAC08246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91588.1; -; Genomic_DNA.
DR RefSeq; NP_196633.2; NM_121110.2.
DR PDB; 4EUK; X-ray; 1.95 A; A=774-922.
DR PDBsum; 4EUK; -.
DR AlphaFoldDB; Q3S4A7; -.
DR SMR; Q3S4A7; -.
DR BioGRID; 16216; 6.
DR STRING; 3702.AT5G10720.1; -.
DR PaxDb; Q3S4A7; -.
DR PRIDE; Q3S4A7; -.
DR ProteomicsDB; 244785; -.
DR EnsemblPlants; AT5G10720.1; AT5G10720.1; AT5G10720.
DR GeneID; 830938; -.
DR Gramene; AT5G10720.1; AT5G10720.1; AT5G10720.
DR KEGG; ath:AT5G10720; -.
DR Araport; AT5G10720; -.
DR TAIR; locus:2159669; AT5G10720.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_104_17_1; -.
DR InParanoid; Q3S4A7; -.
DR OMA; HEDACQT; -.
DR OrthoDB; 27870at2759; -.
DR PhylomeDB; Q3S4A7; -.
DR BRENDA; 2.7.13.3; 399.
DR PRO; PR:Q3S4A7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3S4A7; baseline and differential.
DR Genevisible; Q3S4A7; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IMP:UniProtKB.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Cell membrane; Coiled coil;
KW Cytoplasm; Developmental protein; Ethylene signaling pathway; Kinase;
KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Transferase.
FT CHAIN 1..922
FT /note="Histidine kinase 5"
FT /id="PRO_0000398590"
FT DOMAIN 373..614
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 779..921
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..120
FT /evidence="ECO:0000255"
FT COILED 169..205
FT /evidence="ECO:0000255"
FT COMPBIAS 622..636
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 828
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 376
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 828
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 787..799
FT /evidence="ECO:0007829|PDB:4EUK"
FT STRAND 805..809
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 810..819
FT /evidence="ECO:0007829|PDB:4EUK"
FT STRAND 823..830
FT /evidence="ECO:0007829|PDB:4EUK"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 836..849
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 853..857
FT /evidence="ECO:0007829|PDB:4EUK"
FT STRAND 880..884
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 888..890
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 892..897
FT /evidence="ECO:0007829|PDB:4EUK"
FT STRAND 901..907
FT /evidence="ECO:0007829|PDB:4EUK"
FT HELIX 910..920
FT /evidence="ECO:0007829|PDB:4EUK"
SQ SEQUENCE 922 AA; 103637 MW; 3E5CA8DD7C18DD16 CRC64;
MVCEMETDQI EEMDVEVLSS MWPEDVGTEA DKQFNVEKPA GDLDTLKEVT IETRTIADMT
RLPNLLNSTH QGSSQLTNLV KQWEYMQDNA VRLLKEELKN LDRQREEAEA KELKIIEEYK
FESNEPENVP VLDETSDLFR RFRQKKRDAL VDSKKIEIYE EFDTVAYWKQ KALSLEKMLE
ASTERERRLM EKLSESLKTM ESQSAPVQEL TQNLKRAEGF LHFILQNAPI VMGHQDKDLR
YLFIYNKYPS LREQDILGKT DVEIFHGGGV KESEDFKREV LEKGKASKRE ITFTTDLFGS
KTFLIYVEPV YNKAGEKIGI NYMGMEVTDQ VVKREKMAKL REDNAVRKAM ESELNKTIHI
TEETMRAKQM LATMSHEIRS PLSGVVGMAE ILSTTKLDKE QRQLLNVMIS SGDLVLQLIN
DILDLSKVES GVMRLEATKF RPREVVKHVL QTAAASLKKS LTLEGNIADD VPIEVVGDVL
RIRQILTNLI SNAIKFTHEG NVGIKLQVIS EPSFVRDNAL NADTEEHEQN GLTETSVWIC
CDVWDTGIGI PENALPCLFK KYMQASADHA RKYGGTGLGL AICKQLVELM GGQLTVTSRV
SEGSTFTFIL PYKVGRSDDY SDDQDEFSDM ADQQSEPDDT AEGYFQFKPL LGSIYSNGGP
GISNDFLPHK VMLTSPIKLI NGFVADPSNN TGQSEMLQLE NGGYMDESKL ETSSGHCPES
AHQYENGNGR CFSKESESCS SSQASSEGGT LEMESELTVS SHREEEKAET EVKETSKPKI
LLVEDNKINI MVAKSMMKQL GHTMDIANNG VEAITAINSS SYDLVLMDVC MPVLDGLKAT
RLIRSYEETG NWNAAIEAGV DISTSENEQV CMRPTNRLPI IAMTANTLAE SSEECYANGM
DSFISKPVTL QKLRECLQQY LH
