ID K9VXW5_9CYAN Unreviewed; 1154 AA.
AC K9VXW5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cri9333_1925 {ECO:0000313|EMBL:AFZ12806.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12806.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ12806.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12806.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003620; AFZ12806.1; -; Genomic_DNA.
DR RefSeq; WP_015202923.1; NC_019753.1.
DR AlphaFoldDB; K9VXW5; -.
DR STRING; 1173022.Cri9333_1925; -.
DR KEGG; cep:Cri9333_1925; -.
DR PATRIC; fig|1173022.3.peg.2076; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
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; 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; IPR036641; HPT_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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AFZ12806.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transferase {ECO:0000313|EMBL:AFZ12806.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 440..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 745..861
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 889..1006
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1060..1154
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1017..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 795
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 938
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1099
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1154 AA; 128149 MW; CCF8A7A22E04F84A CRC64;
MYRSLISKYL DSNLPRPHPN RLPTFEPVLL GLTLLFVGLG WLDRWGFLHI LALVLLTYSI
MSPALTKLVA PLLGLFTLLI GIIHFDGLLI NQSLEIGAVA VLGNFIRKFL LGIEWRLASQ
TVLAQLTQAD TTADGVLNQA VTLLREYTCA DAAIALRQLD EYTAEALVCL PKNALPNSLT
NPKLFAEAIA QNRCLYYEDY PNAATASHIL VAKGAKSVAV LPLQNSENSN NLGEVRGAIL
LIWHQQTQIS SYLQQFVESL LGKLRTLLQF RDTILRLDQV QARFSAILET IHQGVVFVDE
SGEQGWINQA ASQQLKLPAG LVEPALIAQA MAMLRNTADN QQEIITQGAK LFTQANAEIR
NWNWVFSQPQ PKVLSISSTA TRVHDVPGRL WLFDDITERY FAQKAFLERT QELFDTNQEL
SKAKAAAEEA TRVKSQFLAN MSHEIRTPMN AIIGMTGLLL NTELTPLQRD FVETTQTSSD
ALLTIINDIL DLSKIESGKL ELENYSFNLR TCIEEALDLL TPKAAGKNIE LVCLISPQVP
IIIWGDSTRL RQILVNLLSN AIKFTEKGEI LLSVNAQEFE KNKKLSKKLD NNLNRQISIQ
FAVKDSGIGI PADRMDRLFK SFSQVDSSTT RHYGGTGLGL AISKQLSEMM GGQMWVESGG
VIAGIPPQEW QPVSNNLLEQ INKENFYTKS NLNQNVNEIF LDATQLQLAN SPSGSTFYFT
IIAEAEANTL AVDLVNSNSD LKGKRLLIVD DNTTNRQILV LQAQSWGMLS YSLESGAKTL
EFLKQGEVFD LAILDMQMPD MDGLTLGKEI RKLSAYKKLP LVMLTSLNGS ESPNYQKVDF
AAFLTKPVKQ SHLYNLLIHI LSEQPVQVKS SRTAAPKINQ HLAEELPLRI LLTEDNVVNQ
KVALHILKRM GYEADIANNG LEALVALRRQ SYDVVLMDMQ MPEMDGLTAT RQICQEWSSE
ERPRIIAMTA NAMQGDRELC LNAGMDDYVS KPIRVDVLIE ALSKCQPKVK TNSFVLTSQD
NNEGNNEDIK TQNSSQALAS SDAIDTKVLQ SFREMVGEDA EAFLAEMIDC YLEDTPKLLK
DINQAIIEAN APNLRRAAHT LKSSSITLGA KNLASLCKEI EAIAKNGHTE SGLAYSQIKC
EYEKVREALL AISN
//
