ID B4VK29_9CYAN Unreviewed; 2020 AA.
AC B4VK29;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_2971 {ECO:0000313|EMBL:EDX77647.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX77647.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX77647.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX77647.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989843; EDX77647.1; -; Genomic_DNA.
DR RefSeq; WP_006098908.1; NZ_DS989843.1.
DR STRING; 118168.MC7420_2971; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_233583_0_0_3; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 7.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 7.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..120
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 146..198
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 199..272
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 274..326
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 323..372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 397..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 466..515
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 518..566
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 567..637
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 640..692
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 727..753
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1317..1590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1610..1727
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1755..1872
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1922..2015
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1469..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1660
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1804
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1961
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2020 AA; 225451 MW; C7C6201E2E15FF17 CRC64;
MFPFFNRLLI DGLIYWFNVA GWLFDFSPIR PVLMYGGVLA VMGLLAIGLV GLRQTQRKRN
ATAFANSPEH LTKTIPTDFA PLFQAIPQAV VVTDTDGFIV KVNSAFNQLF GYPTKALVGQ
PLSQLYANSE EFDPQTMNPD SADFNQSKRI NYQRQTGNIF SSETLNSVVK DREGNVVGIL
WLIRDISDRQ QTELALQASD ERLNLLIDGI KDYAIYLLDT EGKIVSWNAG AQRLKGYSAS
EIIGQSYQCF FLKDDQESGK PEQSLKIAAE TGRFEDEGWR VRRDGSHFWC TTIITALRDE
TGYLRGFAKV TRDITESKQT EVRLQLLERA IAASSNGILI TDPNVPDNPI IFVNPGFERI
TGYSAQEVLG KNCRFLQGDN QQQPGLDKLK AALKNEQDCH VILQNTRKDG TRFWNELSIS
PIRDRHGKLT HYIGIQTDIS ERRQAEQERD RIFGLSVDML CIAGFDGYFR RLNPAWEKTL
GWSEAELLAQ PYLELVHPDD RAVTLTEAEK LTTGKDSIAF ENRYRCRDGS YRWLLWNAKA
LVEEGLIYCV AHDVTERKQA EAALRESEAR FRTMADSAPV LLWVAGTDGR CTFFNRPWLE
FTGRRLEDEL GEGWLEVVHP EDKNNCLQIY SHSFHQRQTF RMEYRMRRAD GEYRWILDTG
VPRFDTNRGF LGYIGSCIDI TDVKESQAAL EYSQSLLSGV LNSSLDGVMA FEAVRDRQGT
IIDFKWLLIN PAAERMVGRT SEELMGQQLL VEMPGNRQDG LFDFYVQVTE TGIPIEREFH
YRHEGIQAWF QIAAVKLGDG FAVTFGDITH RKQAEEALYQ KNSELQAIFN ALPDLYFRLS
QDGTILDYKA TNLGELYVKP EQFLGQSVHN VLPADVSDKI QGAIAQVIQS QSPVSLDYSL
SLETGEQNYE ARLVPFLDNQ IIGIIRNITE RKQIEQQQRQ DEAAIRALYR VAAAPKLTFE
QRLQGLLALG RRHFGHDVGI VSQIEQGRCL VIAAQVPPKS PRQVQAGDTF ELGQTICSET
IHAKEPIAFE SAEDTEWANH QACLTFGIKS YLGTSVKVAG TVYGALCFFS LDQSSTTLTA
NNRSVSPQLL KLMAQWVGHE IERQQARTLL ERQLQRMLLL KQITQEIRQS LDSKHIFQTA
ATQVGQLFGV NRCLIHTYLA KPCPQIPLVA EYLEPGYEST RQQTIPVVGN PHAQAVLAQD
QAVSSENVYI DPQLEGANQL CRQMDLKSML SVRTSYQEQT NGIICLHQCD RFRQWSDDEI
ELLEAVAAQV GIALAQAQLL EQEKQRREEL TLKNLALHKA KREAEVANRA KSEFLAMMSH
EIRTPMNAVI GMAGLLLDTE LTSQQQDFAN TISSSGEALL TIINDILDFS KIESGKLELE
EHPFDVHVCI EEALDLVASQ ATAKGLELAY LIEPFGFAQG QPQTPATVVG DITRLRQILV
NLLSNAVKFT ERGEVVVSVI SRALSGEAGG AEGAEGAEGA EGAEGAEGAG GAGGAEGAGG
AVPVEHLEAE QTYELQFTVR DTGIGIPRDR MNRLFKPFSQ VDASMTRNYG GTGLGLAISK
RLSERMGGRL WAESEVGKGS TFYFTIVVKS DPNSVTAELD TPQPELRGKR LLVVDDNATN
RQIITLQAQS WGMEVTTAAS GEQALNWLAD SEPFDLAVLD WQMPEMDGLT LALQIQALPN
NEQLPLVMLS SVGRQTPYQP DDMPNFAAFL TKPIKQSQLY NIFVTILGRR RISVRPGDRL
SGTLEAEFAQ RLPLSILLVE DVAVNQKVAR QMLQRLGYRA DVANNGQEAL ESLRRKSYQV
VFMDVQMPEM DGLEATRRIR AEWSSACQPW IIAMTAHAMQ GDREQCLQVG MNDYISKPIR
PEALVQALTT YAQVLDQEGR DSIRDHSDED VSVPEITSDS SVTPALDRQV LKDLREIAGD
DYEGLIAEVI DSYLEDSPPR VQAIRSAIAH DDANALHQSA HALKSSSLTI GATGLAKLCA
DLEALGRTGN LEPASTLISQ FDAEYERVVT ALQQEHPRKL
//
