DHKB_DICDI
ID DHKB_DICDI Reviewed; 1969 AA.
AC Q54YH4; O15763;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Hybrid signal transduction histidine kinase B;
DE EC=2.7.13.3;
GN Name=dhkB; ORFNames=DDB_G0277845;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=AX3-1;
RX PubMed=9576830; DOI=10.1006/dbio.1998.8854;
RA Zinda M.J., Singleton C.K.;
RT "The hybrid histidine kinase dhkB regulates spore germination in
RT Dictyostelium discoideum.";
RL Dev. Biol. 196:171-183(1998).
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.
RX PubMed=18216168; DOI=10.1242/dev.018051;
RA Anjard C., Loomis W.F.;
RT "Cytokinins induce sporulation in Dictyostelium.";
RL Development 135:819-827(2008).
CC -!- FUNCTION: Acts in the cytokinin signal transduction pathway that
CC regulates spore germination. Required for the maintenance of spore
CC dormancy. Does not appear to act as a cytokinin receptor. Probably
CC undergoes ATP-dependent autophosphorylation at a conserved histidine
CC residue in the kinase core, which is followed by transfer of the
CC phosphoryl group to a conserved aspartate residue in the receiver
CC domain. {ECO:0000269|PubMed:18216168}.
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}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in growing cells at low levels.
CC Expression increases following initiation of development. Peaks around
CC 12 hours (tipped aggregate stage), and remains at a high level
CC throughout the remainder of development. {ECO:0000269|PubMed:9576830}.
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DR EMBL; AF024654; AAB71889.1; -; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68095.1; -; Genomic_DNA.
DR PIR; T08875; T08875.
DR RefSeq; XP_642228.1; XM_637136.1.
DR AlphaFoldDB; Q54YH4; -.
DR SMR; Q54YH4; -.
DR STRING; 44689.DDB0215358; -.
DR PaxDb; Q54YH4; -.
DR PRIDE; Q54YH4; -.
DR EnsemblProtists; EAL68095; EAL68095; DDB_G0277845.
DR GeneID; 8621437; -.
DR KEGG; ddi:DDB_G0277845; -.
DR dictyBase; DDB_G0277845; dhkB.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_234459_0_0_1; -.
DR InParanoid; Q54YH4; -.
DR OMA; HWILMES; -.
DR PRO; PR:Q54YH4; -.
DR Proteomes; UP000002195; Chromosome 3.
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; IEA:InterPro.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:dictyBase.
DR GO; GO:1904359; P:regulation of spore germination; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IGI: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; IPR000014; PAS.
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; PF13188; PAS_8; 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 TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1969
FT /note="Hybrid signal transduction histidine kinase B"
FT /id="PRO_0000328205"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 967..1188
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1840..1967
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1755..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 970
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1889
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 1059
FT /note="C -> F (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104..1105
FT /note="ES -> VT (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1131
FT /note="Q -> P (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="Q -> R (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1531
FT /note="S -> C (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966
FT /note="K -> N (in Ref. 1; AAB71889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1969 AA; 218999 MW; 9F89BB7943EF592E CRC64;
MEKSEQTNSF ESSNNNNNNI DSNINNNLEN NNNKNNNNNN NNNNNNNNNN NNIENSIDKN
NKEDNSLVGV NSHRKHRTRL KSKKGNKHET KKEIDYKDLL IKLPHNAVSN FNSLENESSD
NLTPPPPINS SPLPLPLSLP LPLSLPLPLP LPLPLPLPLP PNKENIEINM EDIIIPENKI
KNKNNNNNID INNNNNNNNE KQTSIIEMED LDKLKQPKIN EGSTGKKGKS HFFSFLQRGD
KTNSSILKSS EQPTHKKTKT NINTPPDYPI HYFGHHKRFS SSSDEGSDNS KSQHSSVNTP
TLSRHNIDSL PESQQSQKQS QQQSQQPQQQ NKTKQIQQTI LNNNNDNLNE VTPIKKSSLP
TLEVSPIQSN IINNQTTEKH NSGGFTALTS ASAMNHQNQR RYREHHQINH QQQQQQHHRH
YHHHINSGGS SGSSDKFDYV SATGLSTKNG FNPKSLDVDH FPISDKRNNI NIQAPSTPVQ
SRNYPLFTTQ SPKNANSASK SKNKLKNLKR KIASSITGNN PSGISSSAFN HSFSSWNNNN
SVYTGGNSGG GSGGGGSGGG GGGGGGGGGI GTPSSFLDDN NNLNNGENFK NSNSYNNNNG
SNRSISHDEW LRQFYHKHLE RYEKTKAVDY LIIKPWNFIS WILRPSRIAN YQSKILYRRA
YILNFLNLVL FVVYLLSTIL SSNEWFIFAP GILLSVIYFF LGKINNKMYL IAFLTISTAV
AINITSIIYD LTHTRPTDKL IFSWDLLVMI MVPLLFPSIV YSIVILISVA VTYIGLGIYV
QSSHNFYLLD AYDSFGELLR SIIIVFVILM FYTILSSVDL KEIERKESRI QSLFRISNEA
LVVHKDGLIT DANPAFESMF QIKLQDLLYP IQSGIWEFLP ALEGMFEPGA SKLFDNPDMG
VIETTGIDSS GRTFQVEVRT NKATYDGEPV DVISIIDITG RKQLMEADYA LRKAEAANEA
KVIFLTTVSH ELRTPINGVL ASADILERTT LDSTQKEFLN CIKLSGNYLL DLINDILDYS
KIEAGKMEII KYDFSILKML DNSIRIVSKN IYEKGLDLCI FIDPNVPVIV NGDQRRIKQI
LLNFLSNSIK FTNHGQIIIR VKLESDDSTH SLIKFDVEDS GIGIKTEHLN QLFASFSQID
SGNSRKYQGT GLGLSISKRL CKMMGGDVKV KSEFGVGSTF SFTIPCGIPN TTTRFSLQSL
GSAIYMGEDI QGINKPIGKK KYGASGVVGI VIDSNKYTRK SISQYFAILK ISCVDFENKK
EFENYLSTLA TVDQTTNPQV YLVITSIIDI NQLTTNGLPR DRIYHWILME SPNEERKLPL
EFENRFVKPA QFADIVRCLY KIDSINFFIE QMAGSPYKAS KDLQSGGSSN ESGDGGRSLS
GGGGGVGSNG NGNGGGGLDS NISPSELSSS EHQLISTPLS DVNEFEDINL INQSLSGLGP
SAKVLNSTYF NGLSQSSKIY NNNNRNGVGI GNHHHDHYYQ HRHHHSLPPE EIDYDESPFL
FLNKPIRKVY HSQPSTPVTN GIALMDSSSK SPSIPSSSSA SASALSPNSR HSNELGNGKT
TQSFVFSPTS RKFSLNDSFN PSISTIVLPQ VSYSPSMQGG NFPINMESVY KKIESHNNNF
KRSESKPSTP TFLSNQPSPA TSNSPQLLQS PTTSTTGSIN LSPHRSPNIR LPLEVRSGSL
SSLKPLREDE ELESISDDHT SHLKGSSHSI NQQIPSTIQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQKPQQQ QQKPTTTTTT TSTQLPQNIE KTTTTTTTST TKPTATSSSS
SSSKTTKTQQ QQHHPTTTTT TKSEKIEKTA AATTSEKIEK ILLVEDNFVN VKIFSKLLKD
SGYIFDVAHN GVEAVECVKK GAYDLILMDC QMPEMDGFEA TTAIRELEKS NLIESPPSKK
HSHVVIVALT ANSGYKDKQK CLSVGMNDFL QKPIKTSDIL IQMIKKHLN
