ID E0U6I5_GLOV7 Unreviewed; 1426 AA.
AC E0U6I5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cyan7822_1637 {ECO:0000313|EMBL:ADN13628.1};
OS Gloeothece verrucosa (strain PCC 7822) (Cyanothece sp. (strain PCC 7822)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece verrucosa.
OX NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN13628.1, ECO:0000313|Proteomes:UP000008206};
RN [1] {ECO:0000313|Proteomes:UP000008206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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}.
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DR EMBL; CP002198; ADN13628.1; -; Genomic_DNA.
DR RefSeq; WP_013321735.1; NC_014501.1.
DR STRING; 497965.Cyan7822_1637; -.
DR KEGG; cyj:Cyan7822_1637; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3452; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_246952_0_0_3; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000008206; Chromosome.
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 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; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
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; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_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; 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; PF03924; CHASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00065; GAF; 1.
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; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
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; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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, ECO:0000313|EMBL:ADN13628.1};
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:UP000008206};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..198
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 313..358
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 402..454
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 472..515
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 530..582
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 787..1012
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1032..1148
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1181..1298
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1324..1417
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1082
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1230
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1363
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1426 AA; 160192 MW; CBC5DA670A1A5993 CRC64;
MNIFKNLQAD LSKIYQKKNL VFLLTLTFIS LITILIYFSL INQEKIQLKQ QTSSEATLIK
LQIMAEVKSR VLELERLASR WEVRGGTPKR EWELDVNNLL KDYSGYKAIE WVDASNHVRW
VIPVKGNEAA INFNLASQTK RRKALEIAQK NHQSIMTRSV DLIEGGQQFL LYVPLWNSQK
SDGFIVGIFE IESFLNTVLN HQISQGYKIL IFENQELIYS QKPTNFSEKK KWLAEIDLNN
FYSLKWRIQV IPSAEIIAKL NSPLPKVVLV AGLLIGSMLA VALHSTETGR HRSRQLEQEI
LHRQQVEASL REASRLQQAI VDGANYSIIS ANPEGIIQAF NRAAEQMLGY KAEEVVGKFT
PEIIHDPQEI QTRAKELSQE LGMKIEPGFE VLVAKARQGQ KDENIWTYIR KDGSSFSVLL
SITALYDDQG QISGFLGIGS DRTERLQTQK DLENTLRELT FQKSALDEAA IVAITNAKGV
IKYVNDKFCQ LSQYSREELI GNTHRIVKSD HHPPDFFKHL WSTISQGKIW QGEIKNKTKN
GSYYWVDTTI VPFLDVQGKP FQYLAIRFDI TNRKYIEQAL QKELKQTLLL KQISQKIRES
LEPQQIFQTT ADQVGRAFGV NRCLIHSYIP TPTPRIPIVA EYFQPEYDSM MGLDIPVSGN
LHAETLLTTE RAIASDNVFA EPQLKSVAGI CEQMGSKSIL AIRTSYQGKP NGIIGLYQCD
HFRHWTFEER ELLEAIAAQV GIALAQAQLL EQERKQRSEL ALKNIALEGA KREAEAANKA
KSEFVAMMSH EIRTPMNGVI GMTGILLDTP LSELQRDCVE TIRNSGDALL MIINDILDFS
KIESGKLELE EQPFNLRESI ESSLDLLAPK AAEKGLELAY IFDPNTPETI LGDVTRLRQI
LVNLIGNGIK FTEKGEVVVN VSSYPQEKSS TAPTYTIEFA VTDTGIGIAP ERKDKLFKAF
SQVDSSTTRQ YGGTGLGLVI SKRLTQLMGG EISVDSQQGK GSTFKFTITA EAFHSSTLAW
EKYIITHLAN KRVLIVDDNQ TNRKILILQT QSWGMIPTAV DSGQKAIEII AQGETFDLAI
LDMQMPSLDG VMLAQILRQY PSGKNLPLIL LSSAGQLLPI ERLKVDFSST LSKPIHQTQL
YNALVQALQT QTKITLDRPS VPENGSILSK YKDLGQQHPL RILIGEDNAV NQKVIQQILQ
RMSYRADLVA NGLEVIQALK LQSYDVVLMD IQMPEMDGLE TTRWITQTYH QGSRPRIIAM
TANAMQGDQE HCLAAGMDDY LSKPINIFAL AEALQNSQPI TVDTTSKEMV KSLQYLQDSL
CAGDLELMKE MIQCYFIESE KLVKTITSAI AHTDAPSLFR AAHSLKSSSA SLGASHFSEL
CKTLEMIGKT GNLNKAPEMV KILEQEYIKV TQDLKQFLIS TSSNYE
//
