DHKC_DICDI
ID DHKC_DICDI Reviewed; 1225 AA.
AC Q95PI2; O15784; Q554Q0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Hybrid signal transduction histidine kinase C;
DE EC=2.7.13.3;
GN Name=dhkC; ORFNames=DDB_G0274191;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=9808785; DOI=10.1006/dbio.1998.9049;
RA Singleton C.K., Zinda M.J., Mykytka B., Yang P.;
RT "The histidine kinase dhkC regulates the choice between migrating slugs and
RT terminal differentiation in Dictyostelium discoideum.";
RL Dev. Biol. 203:345-357(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RA Anjard C., Loomis W.F.;
RT "The histidine kinases of Dictyostelium.";
RL (In) Inouye M., Dutta R. (eds.);
RL HISTIDINE KINASES IN SIGNAL TRASNDUCTION, pp.1-1, Academic press, San Diego
RL (2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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 [5]
RP FUNCTION, MUTAGENESIS, DEVELOPMENTAL STAGE, AND PHOSPHORELAY INHIBITION BY
RP AMTC.
RX PubMed=16188250; DOI=10.1016/j.ydbio.2005.08.043;
RA Kirsten J.H., Xiong Y., Dunbar A.J., Rai M., Singleton C.K.;
RT "Ammonium transporter C of Dictyostelium discoideum is required for correct
RT prestalk gene expression and for regulating the choice between slug
RT migration and culmination.";
RL Dev. Biol. 287:146-156(2005).
RN [6]
RP FUNCTION, AND PHOSPHORELAY ACTIVATION BY AMTA.
RX PubMed=16835443; DOI=10.1128/ec.00058-06;
RA Singleton C.K., Kirsten J.H., Dinsmore C.J.;
RT "Function of ammonium transporter A in the initiation of culmination of
RT development in Dictyostelium discoideum.";
RL Eukaryot. Cell 5:991-996(2006).
CC -!- FUNCTION: Acts in a signal transduction pathway that regulates the slug
CC versus culmination choice. Believed to be the first component of a
CC phosphorelay that couples the sensing of ammonia to the modulation of
CC PKA activity and hence activates culmination and spore germination.
CC Ammonium transporters amtA and amtC are thought to respectively
CC activate and inhibit dhkC phosphorelay. This protein probably undergoes
CC an ATP-dependent autophosphorylation at conserved His residue in the
CC kinase core, and a phosphoryl group is then transferred to a conserved
CC aspartate residue in the receiver domain. {ECO:0000269|PubMed:16188250,
CC ECO:0000269|PubMed:16835443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during growth and
CC development, with a peak during early aggregation (8 h). Mounds display
CC weak expression within the upper regions and very strong expression at
CC the perimeter of basal cells in contact with the substrate. Expression
CC becomes tip-specific during first finger formation.
CC {ECO:0000269|PubMed:16188250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84206.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF029726; AAB84206.1; ALT_FRAME; mRNA.
DR EMBL; AF361474; AAK50004.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69988.1; -; Genomic_DNA.
DR PIR; T09057; T09057.
DR RefSeq; XP_644273.1; XM_639181.1.
DR AlphaFoldDB; Q95PI2; -.
DR SMR; Q95PI2; -.
DR STRING; 44689.DDB0185038; -.
DR PaxDb; Q95PI2; -.
DR PRIDE; Q95PI2; -.
DR EnsemblProtists; EAL69988; EAL69988; DDB_G0274191.
DR GeneID; 8619701; -.
DR KEGG; ddi:DDB_G0274191; -.
DR dictyBase; DDB_G0274191; dhkC.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_268268_0_0_1; -.
DR InParanoid; Q95PI2; -.
DR OMA; MGGKIWC; -.
DR PRO; PR:Q95PI2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0061128; P:positive regulation of chemotaxis to cAMP by DIF-2; IMP:dictyBase.
DR GO; GO:0060359; P:response to ammonium ion; IMP:dictyBase.
DR GO; GO:1903831; P:signal transduction involved in cellular response to ammonium ion; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
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; 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; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Transducer; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..1225
FT /note="Hybrid signal transduction histidine kinase C"
FT /id="PRO_0000328269"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 426..653
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 669..784
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1078..1200
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 313..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 429
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1127
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1225 AA; 137347 MW; 4BB546254BF7EF16 CRC64;
MIVEVELGFL LSTLFFTIIS IILFYFFINN KNNLIDQCQE VTKLNNKDNK IVNNNNNNYN
NNNFNKIEEI NDDKNKEIIK LINNSNNKNL KIKIQEIDSG NNNNNNNNNN NNNNNNLNKN
SNEIFRNFKI FSGSLLVIDQ DLNIISSSES VRDIFSNIND INGVNQQVIG SLQNYSFINL
VHQKDKDRVS TFLKLKFKNN NNIKHQQFSE DIINEKDELK EIQIEDNKEL IIINNNNNNN
NDNVLKFGNN NSNNSSIILF QGVYHLNNTD LSKPFNLQVS ILPFISENYI VLSLKDLSPP
PLRLLLNKTS SALSPRSLSS SSSSSPSSSN NNGNTNNSGS LSPRSSNSNG SAVSPRNVSS
NSMSPRGQNS DRSISSPRGS SSSSSSSSNE LAISPRNSNG TISSPRTSNL SIESVLNNKS
IDMISHLSHE LRTPIHSVIA SIQLFRSTIL TVTQNEYLSI IDTSANTLLE LVSNVLDYKR
IRSGKLTLNN VDFNLCHVIE DVCAMVSPQA QAKSLQIASF IFIHCPLSFY GDPIRLRQVL
LNLIGNGLKY TNKGQVCISV EPEQVNEHCM YLHFQVKDSG IGIKEENMSK LFAGFSQVNN
GGTTQEALGS GLGLAISKDL VELMGGKIWC SSNATQNNGE AGCTFHFVIP LETNPKQLPC
PIQNFNGLSV LVVDKNPYIQ TVLCQYLEGW NCQVIKSSDI KEASNKLKDL RREQIEVVMI
DIDNIDFRDF IQFKDAFNRL EFGRIGLITM SSDRSMVNEM GFGTSKLTKP FRQSHLVACL
LASMPEHSSS TTNCFSNIVG MNSNINNNNN INNNSNNNNN NMQTHNSNSV YGNGNYGNCT
PFSNNNNRIH MMSSGDKPSI NNRRMSISLG KIPTFNSGGS NSPRSKKLFE EVLQQQQLQQ
QLQQQLQQQQ QLQQQQQQQQ QQQQQQQQQL QQQQQQLNTI DDDSNNYCNT TGTMDSIDEI
NKNNYSDSES DELNDDQAPI IAPVQQLSFG RVTRRHSIDI IMFENSRELS ELRNLEDSTR
YLSPRSMNNN NGNNDNGING GSGNSLFGSS IKEEIGGTSD TSSLAQSPNS LSPRAPTKIM
ILDDNPVSLK LMQRILESRG FECYPFDCSE KAVAQLDQVN PAIIFMDCEM PKMNGFECTQ
LIRKREQESL CLLKDRKIII ALTAHINPEI QVKCFDAGMN DFISKPFKPQ CLELILRKWE
DCISNNQLNY NNSLINNQTT IQEQV
