Reviewed, UniProtKB/Swiss-Prot Q54YH4 (DHKB_DICDI)

Names and origin

Protein names

Recommended name:
    Hybrid signal transduction histidine kinase B
    EC=2.7.13.3

Gene names

Name:	dhkB
ORF Names:	DDB_G0277845

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts in the cytokinin signal transduction pathway that regulates spore germination. Required for the maintenance of spore dormancy. Does not appear to act as a cytokinin receptor. Probably undergoes ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, which is followed by transfer of the phosphoryl group to a conserved aspartate residue in the receiver domain. Ref.3
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Developmental stage	Expressed in growing cells at low levels. Expression increases following initiation of development. Peaks around 12 hours (tipped aggregate stage), and remains at a high level throughout the remainder of development. Ref.1
Sequence similarities	Contains 1 histidine kinase domain. Contains 4 LRR (leucine-rich) repeats. Contains 1 response regulatory domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Leucine-rich repeat Repeat Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1969	1969	Hybrid signal transduction histidine kinase B		PRO_0000328205
Regions
	Transmembrane	660 – 680	21	Potential
	Transmembrane	684 – 704	21	Potential
	Transmembrane	708 – 728	21	Potential
	Transmembrane	747 – 767	21	Potential
	Transmembrane	795 – 815	21	Potential
	Repeat	294 – 317	24	LRR 1
	Domain	967 – 1188	222	Histidine kinase
	Repeat	996 – 1019	24	LRR 2
	Repeat	1031 – 1054	24	LRR 3
	Repeat	1422 – 1446	25	LRR 4
	Domain	1840 – 1967	128	Response regulatory
	Compositional bias	14 – 19	6	Poly-Asn
	Compositional bias	30 – 52	23	Poly-Asn
	Compositional bias	124 – 127	4	Poly-Pro
	Compositional bias	182 – 188	7	Poly-Asn
	Compositional bias	192 – 199	8	Poly-Asn
	Compositional bias	280 – 283	4	Poly-Ser
	Compositional bias	342 – 349	8	Poly-Asn
	Compositional bias	411 – 416	6	Poly-Gln
	Compositional bias	537 – 540	4	Poly-Asn
	Compositional bias	549 – 571	23	Poly-Gly
	Compositional bias	596 – 599	4	Poly-Asn
	Compositional bias	1381 – 1387	7	Poly-Gly
	Compositional bias	1390 – 1397	8	Poly-Gly
	Compositional bias	1461 – 1466	6	Poly-Asn
	Compositional bias	1473 – 1485	13	His-rich
	Compositional bias	1536 – 1543	8	Poly-Ser
	Compositional bias	1719 – 1755	37	Poly-Gln
	Compositional bias	1758 – 1762	5	Poly-Gln
	Compositional bias	1765 – 1773	9	Poly-Thr
	Compositional bias	1782 – 1791	10	Poly-Thr
	Compositional bias	1797 – 1803	7	Poly-Ser
	Compositional bias	1809 – 1812	4	Poly-Gln
	Compositional bias	1816 – 1821	6	Poly-Thr
Amino acid modifications
	Modified residue	970	1	Phosphohistidine; by autocatalysis By similarity
	Modified residue	1889	1	4-aspartylphosphate By similarity
Experimental info
	Sequence conflict	1059	1	C → F in AAB71889. Ref.1
	Sequence conflict	1104 – 1105	2	ES → VT in AAB71889. Ref.1
	Sequence conflict	1131	1	Q → P in AAB71889. Ref.1
	Sequence conflict	1148	1	Q → R in AAB71889. Ref.1
	Sequence conflict	1531	1	S → C in AAB71889. Ref.1
	Sequence conflict	1966	1	K → N in AAB71889. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54YH4-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 9F89BB7943EF592E	FASTA	1,969	218,999
	10 20 30 40 50 60 MEKSEQTNSF ESSNNNNNNI DSNINNNLEN NNNKNNNNNN NNNNNNNNNN NNIENSIDKN 70 80 90 100 110 120 NKEDNSLVGV NSHRKHRTRL KSKKGNKHET KKEIDYKDLL IKLPHNAVSN FNSLENESSD 130 140 150 160 170 180 NLTPPPPINS SPLPLPLSLP LPLSLPLPLP LPLPLPLPLP PNKENIEINM EDIIIPENKI 190 200 210 220 230 240 KNKNNNNNID INNNNNNNNE KQTSIIEMED LDKLKQPKIN EGSTGKKGKS HFFSFLQRGD 250 260 270 280 290 300 KTNSSILKSS EQPTHKKTKT NINTPPDYPI HYFGHHKRFS SSSDEGSDNS KSQHSSVNTP 310 320 330 340 350 360 TLSRHNIDSL PESQQSQKQS QQQSQQPQQQ NKTKQIQQTI LNNNNDNLNE VTPIKKSSLP 370 380 390 400 410 420 TLEVSPIQSN IINNQTTEKH NSGGFTALTS ASAMNHQNQR RYREHHQINH QQQQQQHHRH 430 440 450 460 470 480 YHHHINSGGS SGSSDKFDYV SATGLSTKNG FNPKSLDVDH FPISDKRNNI NIQAPSTPVQ 490 500 510 520 530 540 SRNYPLFTTQ SPKNANSASK SKNKLKNLKR KIASSITGNN PSGISSSAFN HSFSSWNNNN 550 560 570 580 590 600 SVYTGGNSGG GSGGGGSGGG GGGGGGGGGI GTPSSFLDDN NNLNNGENFK NSNSYNNNNG 610 620 630 640 650 660 SNRSISHDEW LRQFYHKHLE RYEKTKAVDY LIIKPWNFIS WILRPSRIAN YQSKILYRRA 670 680 690 700 710 720 YILNFLNLVL FVVYLLSTIL SSNEWFIFAP GILLSVIYFF LGKINNKMYL IAFLTISTAV 730 740 750 760 770 780 AINITSIIYD LTHTRPTDKL IFSWDLLVMI MVPLLFPSIV YSIVILISVA VTYIGLGIYV 790 800 810 820 830 840 QSSHNFYLLD AYDSFGELLR SIIIVFVILM FYTILSSVDL KEIERKESRI QSLFRISNEA 850 860 870 880 890 900 LVVHKDGLIT DANPAFESMF QIKLQDLLYP IQSGIWEFLP ALEGMFEPGA SKLFDNPDMG 910 920 930 940 950 960 VIETTGIDSS GRTFQVEVRT NKATYDGEPV DVISIIDITG RKQLMEADYA LRKAEAANEA 970 980 990 1000 1010 1020 KVIFLTTVSH ELRTPINGVL ASADILERTT LDSTQKEFLN CIKLSGNYLL DLINDILDYS 1030 1040 1050 1060 1070 1080 KIEAGKMEII KYDFSILKML DNSIRIVSKN IYEKGLDLCI FIDPNVPVIV NGDQRRIKQI 1090 1100 1110 1120 1130 1140 LLNFLSNSIK FTNHGQIIIR VKLESDDSTH SLIKFDVEDS GIGIKTEHLN QLFASFSQID 1150 1160 1170 1180 1190 1200 SGNSRKYQGT GLGLSISKRL CKMMGGDVKV KSEFGVGSTF SFTIPCGIPN TTTRFSLQSL 1210 1220 1230 1240 1250 1260 GSAIYMGEDI QGINKPIGKK KYGASGVVGI VIDSNKYTRK SISQYFAILK ISCVDFENKK 1270 1280 1290 1300 1310 1320 EFENYLSTLA TVDQTTNPQV YLVITSIIDI NQLTTNGLPR DRIYHWILME SPNEERKLPL 1330 1340 1350 1360 1370 1380 EFENRFVKPA QFADIVRCLY KIDSINFFIE QMAGSPYKAS KDLQSGGSSN ESGDGGRSLS 1390 1400 1410 1420 1430 1440 GGGGGVGSNG NGNGGGGLDS NISPSELSSS EHQLISTPLS DVNEFEDINL INQSLSGLGP 1450 1460 1470 1480 1490 1500 SAKVLNSTYF NGLSQSSKIY NNNNRNGVGI GNHHHDHYYQ HRHHHSLPPE EIDYDESPFL 1510 1520 1530 1540 1550 1560 FLNKPIRKVY HSQPSTPVTN GIALMDSSSK SPSIPSSSSA SASALSPNSR HSNELGNGKT 1570 1580 1590 1600 1610 1620 TQSFVFSPTS RKFSLNDSFN PSISTIVLPQ VSYSPSMQGG NFPINMESVY KKIESHNNNF 1630 1640 1650 1660 1670 1680 KRSESKPSTP TFLSNQPSPA TSNSPQLLQS PTTSTTGSIN LSPHRSPNIR LPLEVRSGSL 1690 1700 1710 1720 1730 1740 SSLKPLREDE ELESISDDHT SHLKGSSHSI NQQIPSTIQQ QQQQQQQQQQ QQQQQQQQQQ 1750 1760 1770 1780 1790 1800 QQQQQQQQQQ QQQQQKPQQQ QQKPTTTTTT TSTQLPQNIE KTTTTTTTST TKPTATSSSS 1810 1820 1830 1840 1850 1860 SSSKTTKTQQ QQHHPTTTTT TKSEKIEKTA AATTSEKIEK ILLVEDNFVN VKIFSKLLKD 1870 1880 1890 1900 1910 1920 SGYIFDVAHN GVEAVECVKK GAYDLILMDC QMPEMDGFEA TTAIRELEKS NLIESPPSKK 1930 1940 1950 1960 HSHVVIVALT ANSGYKDKQK CLSVGMNDFL QKPIKTSDIL IQMIKKHLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The hybrid histidine kinase dhkB regulates spore germination in Dictyostelium discoideum." Zinda M.J., Singleton C.K. Dev. Biol. 196:171-183(1998) [PubMed: 9576830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, DEVELOPMENTAL STAGE. Strain: AX3-1.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Cytokinins induce sporulation in Dictyostelium." Anjard C., Loomis W.F. Development 135:819-827(2008) [PubMed: 18216168] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF024654 Genomic DNA. Translation: AAB71889.1. AAFI02000023 Genomic DNA. Translation: EAL68095.1.
PIR	T08875.
RefSeq	XP_642228.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3393168.
GenomeReviews	Gene locus dhkB in contig CM000152_GR.
KEGG	ddi:DDB_0215358.
Organism-specific databases
dictyBase	DDB_G0277845. dhkB.
Enzyme and pathway databases
BRENDA	2.7.13.3. 424.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR000014. PAS. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
ProDom	PD000039. Response_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. SM00091. PAS. 1 hit. SM00448. REC. 1 hit. [Graphical view]
TIGRFAMs	TIGR00229. sensory_box. 1 hit.
PROSITE	PS50109. HIS_KIN. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHKB_DICDI

Accession

Primary (citable) accession number: Q54YH4
Secondary accession number(s): O15763

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	October 13, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)