ID DHKA_DICDI Reviewed; 2150 AA.
AC Q54U87; Q23863;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Hybrid signal transduction histidine kinase A;
DE EC=2.7.13.3;
GN Name=dhkA; ORFNames=DDB_G0280961;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS, CHARACTERIZATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=8670894; DOI=10.1002/j.1460-2075.1996.tb00763.x;
RA Wang N., Shaulsky G., Escalante R., Loomis W.F.;
RT "A two-component histidine kinase gene that functions in Dictyostelium
RT development.";
RL EMBO J. 15:3890-3898(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-1396 AND ASP-2076,
RP INTERACTION WITH SDF-2, AND SUBCELLULAR LOCATION.
RX PubMed=10373524; DOI=10.1128/mcb.19.7.4750;
RA Wang N., Soderbom F., Anjard C., Shaulsky G., Loomis W.F.;
RT "SDF-2 induction of terminal differentiation in Dictyostelium discoideum is
RT mediated by the membrane-spanning sensor kinase DhkA.";
RL Mol. Cell. Biol. 19:4750-4756(1999).
RN [4]
RP FUNCTION.
RX PubMed=15897458; DOI=10.1073/pnas.0501820102;
RA Anjard C., Loomis W.F.;
RT "Peptide signaling during terminal differentiation of Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7607-7611(2005).
CC -!- FUNCTION: Acts as a receptor histidine kinase for the cytokinin SDF-2
CC in a signal transduction pathway that regulates prestalk gene
CC expression and controls terminal differentiation of prespore cells.
CC Binding of SDF-2 to this protein inhibits phosphorelay and induces
CC rapid sporulation. This protein undergoes an ATP-dependent
CC autophosphorylation at a conserved histidine residue in the kinase
CC core, and a phosphoryl group is then transferred to a conserved
CC aspartate residue in the receiver domain. {ECO:0000269|PubMed:10373524,
CC ECO:0000269|PubMed:15897458}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10373524};
CC -!- SUBUNIT: Interacts with SDF-2, an acbA peptide involved in sporulation.
CC {ECO:0000269|PubMed:10373524}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 8 hours following initiation of
CC development, prior to the appearance of mound tips. Subsequently
CC persists throughout development. {ECO:0000269|PubMed:8670894}.
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DR EMBL; U42597; AAC47300.1; -; mRNA.
DR EMBL; AAFI02000040; EAL66777.1; -; Genomic_DNA.
DR PIR; S71629; S71629.
DR RefSeq; XP_640889.1; XM_635797.1.
DR AlphaFoldDB; Q54U87; -.
DR SMR; Q54U87; -.
DR STRING; 44689.Q54U87; -.
DR PaxDb; 44689-DDB0215354; -.
DR EnsemblProtists; EAL66777; EAL66777; DDB_G0280961.
DR GeneID; 8622946; -.
DR KEGG; ddi:DDB_G0280961; -.
DR dictyBase; DDB_G0280961; dhkA.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_231770_0_0_1; -.
DR InParanoid; Q54U87; -.
DR OMA; SIMEIEC; -.
DR PRO; PR:Q54U87; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:dictyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; TAS:dictyBase.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:dictyBase.
DR GO; GO:0009784; F:transmembrane receptor histidine kinase activity; IDA:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IGI:dictyBase.
DR GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Cytokinin signaling pathway;
KW Developmental protein; Differentiation; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..2150
FT /note="Hybrid signal transduction histidine kinase A"
FT /id="PRO_0000328204"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1098..1118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 838..1082
FT /note="CHASE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT DOMAIN 1235..1317
FT /note="PAS"
FT DOMAIN 1321..1376
FT /note="PAC"
FT DOMAIN 1393..1620
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 2026..2146
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1139..1164
FT /evidence="ECO:0000255"
FT COMPBIAS 16..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1962..2012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1396
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 2076
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 1396
FT /note="H->Q: Impaired function. Normal function; when
FT associated with N-2076."
FT /evidence="ECO:0000269|PubMed:10373524"
FT MUTAGEN 2076
FT /note="D->N: Impaired function. Normal function; when
FT associated with Q-1396."
FT /evidence="ECO:0000269|PubMed:10373524"
FT CONFLICT 1319
FT /note="S -> A (in Ref. 1; AAC47300)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509
FT /note="L -> R (in Ref. 1; AAC47300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2150 AA; 239636 MW; 1FDA618EE9B3DBCA CRC64;
MELKTFKDLN DDIIGDTSPV INTGDQPNPL RTQQQQLQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQHHIP QQLYQKQQQQ QHSHSYGNHS FIHNVSPTSP SYDINNNNNN NNNNNNNNNN
NNNNNNNSNN NNNNNNNNKN NYNNNYYYSP IENSNISKSL EESVLNQFPH NFNLNSSNNN
YLNNSSSLHN INQSVNSLSN NNNNQTNQQP INNNNNNNNN NNNNNSNNSN NSNNNNNGNN
NNNITDSPTK SKRHSTYETN IGSHQRRKSI QSLIANSAIH SFSKLKNKPL SSSTPSTVNT
CGAVNNNSNN NNNNNNNSTG SLGAIPMDRS FDGNINTITE ESTGGNNSPR SNCGSNCGSN
GGIPLSPRNL SSLNSGVNVS PRNIHLNNLN NNSSNLPPLS PRHINFHINV SNLNNNNNNN
INPNNNPNNS NNSNNNVSPR NNNHNISPRG SNISPRSNNG GSTTISPRNI SNNNNIINNI
NNNNILTPPR NSPRLENVNP TNSPRLLATS LNSTLPIVSS LTSSNNNNQS NNNTNPSINN
NNGRNGHCIQ TISEEILGNK PVVYNNGNNN NNNNTNNSTT SNNNITTNNN NNNNNNINNN
VLSTPRKRTK GNHSKTNSLQ DFETSSMNGG DDSISGAGSG GSLRRRNKDD NDENDGNSNN
TNSNNSNNNN NNNNNSSNNN NNNSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNYHN GATMMMSHNH QSIGMSSSPK KNNFKPFSRN CSLMGMGRRA WAIILGLFIV
GSSISILATL VLRYSEENSI ADDFARVARD RFTMLRIEFN NRLYITQTLS LLLSVFPSTS
EDQFVPFSKL WSDNAEGLEG IMWAPRVSNL DRYTWEIEHS VKIREIVTNP NNSSDMRDVP
AAAASDYYPI LFSEPQSSND HFKGYNIYSD MWRRPSLNKT RDTGEKVSVA SPYINKLANV
PKNSRSNVLL YIYQAVYTYG KVLSTVEDRR HEVIGFASCR FFISRMVSAS LQRLTEEDSL
DLYVFDLDST PIGELIYYRA SNAGNDDGSS PTNIMNGKML EDRSDMIYYN TMNVGGRNWM
IALRPSRKFT NKHYTFYPYA IGGVCMLLSA LVSFWFAVNT KHNIKLSATN EDLHKEIYNR
KLAEKALAES QERLELAMEG SEDAVWDWKV NTGELHISSR WFQILKAHDT SYQSRTLYEE
LKSSSTNNLN FKGDSKNGGS NNGTFNLFKN GKVDSSSPQS ITNVNTTNGG GGGELRKSNS
GYLYNDELFS PIILEEMVSS PNTHQLAIWN MKFLAELIHP DDKQKFISEI KKTITRETSI
MEIECRMRKK YGGYLYIIMR GKVVSNETSF KDNSLRMAGT LRDMTSRKDM QRLILEKEAA
EEANKAKSAF VATVSHEVRT PLSGVIGVSD LLLETNLSEE QRDYVQTIQK SSQALLTIIN
DILDYSKLES RQLKMETLPF SIIETCQAVI HMLSVAANDD VDILLRVPPN VPRIIFGDAM
RMRQVLLNLL SNAIKFTSRG HVLTDISVDD SIPPTNTEEE IIHLCITIED TGIGIPQSLF
DSIFEPFSQA DNSTTRKYGG TGLGLSITKR LIEEVMGGTI QVSSIVGQGS KFKCIIPFLL
PNTSPSDLNL ISPSSLPKPF INRSPKSTYS FTDKKNSVPS TPIPSGDILI NKVCLLICRD
TVTELVFKEQ LEWLGMIVKQ VPRNVIDSIK NTILNNNNNN NNNNNNNNNN SNNSSSIISP
SSLDYSDENE HLDLVLIDLE ILTEHLKIPS NVPIIFITPT KFNISKHNGI LNKWITKSPN
QRVELIRRPA ITDKLIPIIS KCIKSQVQFT SGSSQLQSQQ ANLQQQLLHQ QLCNNGQTLN
NNYNSGGIGG GGGGGGSNTM NGSSGNLSNN NNFGQTPLSS GLVLLVHTGR TPPLFNNNGN
SIIPPLELAV DHHGNQQQQL YQQQQQQQNN SSGNFQQFYQ QQNNNSNNSF TPTLPNENSN
NSIMNNSLNN NNTTPSNVTP TLFTSSPLDL QGRDTPVLQP PAYRKKALIV EDNELNRKVL
AQLFKKIDWT ISFAENGREA LKEITGERCF DIVFMDCQMP VLDGFQTTKI IRSKERENNW
KRMNIVALSA GSSSSFVQDC LDSGMDSFMG KPITLATLKD ALAKWGGYNN
//
