ID B4VIH4_9CYAN Unreviewed; 1946 AA.
AC B4VIH4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_7722 {ECO:0000313|EMBL:EDX77984.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX77984.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX77984.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX77984.1,
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; DS989842; EDX77984.1; -; Genomic_DNA.
DR STRING; 118168.MC7420_7722; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_001440_0_0_3; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 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; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01590; GAF; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 3.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 3.
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); 2.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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}.
FT DOMAIN 110..170
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..330
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 497..553
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 634..685
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 705..841
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 891..1027
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1262..1496
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1516..1633
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1661..1778
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1833..1938
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 327..357
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1225..1255
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1566
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1710
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1880
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1946 AA; 218564 MW; 5F7CFAB2E0233FB4 CRC64;
MFQLQPAPYP IIMQPDITAI TLPALEHFID YHPLTIEAQA TLVEAIALLN QGQSLSAYQS
GQIAKEPERS HRCVLVTENS ALIGIVTTRK LIELMLAGVN FQDTQVADVM MRSPVTLTLS
ESCHLFTALS LFESYSIDHL PVLDKTGKLI GLITENSICQ GLPELNLLKS QSVAATMTTP
GLNVSLTTSI LDVAQQLIKT QETCAVLIQE TVIGDETNGR RFKKSAIASP LSSVSAHSLP
VGLITEQDLI HCLQLSVFGL DLSKTPVSMV IKKPLLSLHP DDSIKQGLEQ MRQVGQTPQL
VYQSPENLLG IFTATDIIKA LNPLALLNQV EQLQQTINQQ ANQLQQTLND LNQAETTVET
SHQRLQLIQT IASNPTLNGK DWQTEFSELT EVPSASRCLP SSSLVETPGD HAMEPPQVAH
IVKTATERLE LILRASQDGF WDWNMITGDI YFSPRWKEML GYADWELPNE LASWEKVIFE
EDRIAALKLI EDYNSGKVSR FQAVQRFHHK NGSTVYILSR AIHQKDTADR VIRMVGTHTD
ITDRKQAEAT LQAEYSFKTQ LIERMGEGVC VCHSIETYPY IRFTVWNQQM VEITGYTVDE
INRRGWYQTF YPDPKQRSQA VKRVAQMQRG EDLVAEEWDI VRADGSHRIL SISTSRIETS
ENQTHILALI QDVTERLHSE TASQQQAERE RLIRAIALRI HQSLELEDIL HTTVTEVRHF
LQTDRVLIYR FNPDWSGVVA VESVESETLS MLGQTIYDPC FGEKSAVRYQ QGYINTLEDT
HTADIATCYR DFLADLHVRA NLVVPILQGS QLWGLLIAHH CHHPRHWQTV DIDLLQQLAT
QVAIAIQQSE LYQQLSTELV ERKQAETALR QQAERERLIS AIARRIRQSL HLTEILNTTV
TEVRHFLQTD RVLIYRFNPD WSGVVEVESV AVKELSVLGR TIFDPCFGEK SAVRYQKGDI
HTLEDIHTAN LESCYRNFLA NLQVRANLVV PIIQGQKLWG LLIAHHCNQP RHWQPQETEL
LVQLATQVAI AVQQSELYQQ AQADLSERQQ AETALQQQLQ RSLLLKQITQ DIRQSLDAQQ
IFQTTATQIG QAFRVNRCVI HTYVASPAPQ IPFVAEYLEP GYSSILTVKI PVANNPHIQQ
VLAADRAIAS NNVYDDPLLQ NATGMCDQVN LKSMLVVRTS YKEKPNGVIC LHQCDQFRQW
SNDEIELLEA VADQVGIALA QAQLLEQEKH QRQQLAEQNV AMEKAKQIAE AANRAKSDFL
ATMSHEIRTP MNAVIGMTGL LLDTQLSHEQ AEFAETIRNS GEALLTIIND ILDFSKIESG
KLELEEQPFN LRTCIEESLD LLTPKAAEKA IELAYLFDPH TPNTIRGDIT RLRQILVNLL
SNALKFTHQG EVTVSVSSKR VSPQSLEQLS HRTNKEQQYE ILFAVKDTGI GIPPDRLDRL
FKAFSQVDSS TSRHYGGTGL GLVISKRLSE MMGGRIWVES EVGKGSIFYF TIVAPVCHID
NLSNLDLRQP QLEGKRMLIV DDNATNRRIL TLQGQSWGVL TRAAESGEQA LDWLQQGETF
DLAILDMHMP GMDGVNLASQ IRRQPDGQEI PLVMLTSIGK PENSGQLDEA KFAAFLTKPI
KQSQLYNVLM DVLVGQPVKV RSTCEISPTI DPYMGANIPL RILLAEDNVV NQQVGLHILG
RMGYRADVAA NGLEVLEALH RQSYDVVLMD VQMPEMDGLK ATQRICQEWS AENRPHIIAM
TANAMRGDRE TCLQAGMDDY ISKPIRVEEL VRSLQGVPKK VQETRSFQKA EAREQRLQAK
KQGSKVQGNN NGLDGHDVID DHAFQQLCDM VKDDQVLIQV IDSFLDEGAQ LLGVMNQALD
SQKTNTLSPE TLTTCQQAAH SLKSTSGTVG AINLSELCKH LETIDIEDET DNPLTLTSRL
LTQIDQEYEQ VKVALQSKRQ QLKEKC
//
