ID K9T2Q4_9CYAN Unreviewed; 1146 AA.
AC K9T2Q4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ple7327_1822 {ECO:0000313|EMBL:AFY77172.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY77172.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY77172.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY77172.1,
RC ECO:0000313|Proteomes:UP000010382};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-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};
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DR EMBL; CP003590; AFY77172.1; -; Genomic_DNA.
DR RefSeq; WP_015143476.1; NC_019689.1.
DR AlphaFoldDB; K9T2Q4; -.
DR STRING; 118163.Ple7327_1822; -.
DR KEGG; plp:Ple7327_1822; -.
DR PATRIC; fig|118163.3.peg.2014; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR HOGENOM; CLU_000650_6_0_3; -.
DR Proteomes; UP000010382; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFY77172.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010382};
KW Transferase {ECO:0000313|EMBL:AFY77172.1}.
FT DOMAIN 421..678
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 680..824
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 852..969
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1015..1132
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 85..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..375
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 902
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1065
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1146 AA; 126261 MW; DFD36A868E71BE1F CRC64;
MSRDPKQNDR ADNFLGDREI AELLDNLEDS PTSASANGSL DDFGSLFNED FSTDSTDSGM
LSDNLPDRIT FSELPSDDEI SKIFSEDLSW KEDRSSSPER DRWLDFSAPE TQSQENVTTS
ASDFLNDELA TFLSEESFDG NSVQPIAAES PSLDDELATF LSEESFDGNV ADDTNTTPQS
SDWDELKQLL AGDDLEETYS PTAGDSPAIP APTPVTEEES LALGESDLDD LAALLEEPTT
ASASRTLEPN IFEDLEAVLG DFPATMNDPS PSNKNNRSDD EFQDLEKLLE KAEGTISPSP
AAQPASIAPR LQARTRVPKA KLFDQTMRVP VKQLDNLSNL IGELVVKRNA LEDDQERLRQ
SLDNLLNQVQ ALSEMGARMH DLYERTLLEG ALLASRNQNN SFAGSGSNAF PTSNADASSG
NASYPIDREL DALEIDRFTG FHLLSQEMIE LIVRIRESTS DIQFLVDDTD QVTRTLRQVT
TQLQEGMTKS RMVPFAQTAD RLPRAIREVS MRLNKQAKLY VEGKDVLIDK MILEQLYNPM
THLVNNAIAH GIETPEERIK NGKPPEGRVT VRAFIQGNQT VITVSDDGAG INPERVKFKA
IEKGLITQAQ ARTLSKQEVY DFLFHPGFST KDKADDFAGR GVGLDVVYTN LSEIRGTVSI
DSAIGKGTTF TIRLPLTLSI CKALCCESER SRIAFPIDGV EDTKDYSPSE LFTDEEGRKC
IRWREMELPI YRLSELLNYN RQASRRASYA NKPPEELLSI VVLRSAGNLL ALQIDRAIGE
QEIVIKQIEG PIPKPAGIAG ATVLGDGSVM PIGDVLELIE IAQGRMRTDS SGSLWKKTYV
PIQEEGVRSE PTVLIVDDSI TVRQLLSLSF SKAGYRVEQA RDGQEALEKL QSGLPCDIVF
CDIEMPRMNG LELLSHLQQD ARLSEIPLAL LTSRGAQRHR TVAAKLGASG YFTKPYTEKD
LLDAAARMLK GEVLLPGSTK TPRASNPAAD NFSEAEVSFP GLSTIEPRSA KSENLVLIVD
DSVMVREMLS MTFNKAGYRV EPARDGQEAW EKLRGGLPCD LILCDIEMPR MNGLELLSRL
QEDEKLSAIP MAMITSRGAQ KMQNLAAEKG AKGYFVKPYI EEVLLDAAKR LIAGEVLLKK
GSAVEE
//
