ID K9T3N7_9CYAN Unreviewed; 954 AA.
AC K9T3N7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ple7327_1670 {ECO:0000313|EMBL:AFY77033.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY77033.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY77033.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY77033.1,
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003590; AFY77033.1; -; Genomic_DNA.
DR RefSeq; WP_015143338.1; NC_019689.1.
DR AlphaFoldDB; K9T3N7; -.
DR STRING; 118163.Ple7327_1670; -.
DR KEGG; plp:Ple7327_1670; -.
DR PATRIC; fig|118163.3.peg.1844; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_10_3; -.
DR Proteomes; UP000010382; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFY77033.1};
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:UP000010382};
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..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 380..432
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 486..721
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 747..863
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 434..486
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 796
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 954 AA; 107021 MW; 49DC0D86B61A5CC0 CRC64;
MKLSQPIATP KEQAQQFRGI PLRLVLVLPF VLQVVSAVGL VGYLSFKNGQ EAVNDLADRL
MDKSSSLVFK HLDNYLETPQ KINQINLDAI ALGLLDLKDF KTAGHYFWKQ LQTHPDVSYM
AYALTTGEYA GAGKFLAGQG VTIDELSPAT KWKSYTYATD SQGNRTEIVA VYHDYDPKTE
NWYEDAIKAG KPIWGSVYNW DGENLAGYIS ITATSPIYTQ KHQLVGVIGV DLLLASISDF
LQQLKISPTA KTFIVERNGL LIASSSTEKP FTLVNGVAKR LSALNSSDER IQATAKYLQQ
KFSNFQAIKD KQKLDFQLQG KRQFVRVTPW KDEFGLDWLV VITIPESDFM AQINANTQTT
ITLCFVALLI AVLLGLITSR WITQPILRLG KASVAIAQGD LNQRVEVKGI IELSVLSHSF
NEMAQQLQAS FANLALSNQL LDRVNQELEK SNQELETRVE QRTAELQQAK EVAERANRAK
SDFLANMSHE LRTPLNAILG FSQLLNRETS LTKQQQENIG IINRSGEHLL SLINDVLDLA
KIESGKMALY PTDFDLYALL DLIEEMLALR AESKGLQFII ERSNDLPRYI NTDDKKLRQV
LINLLGNAIK FTHEGSVILR ASSVMSHDSL ARNHKEQRIN DQGQTTIYFE IEDTGAGIAP
EEIDTLFEAF VQTETGKQSQ QGTGLGLPIT KKFVELMGGT ITVSSKVGQG SIFKFNIQAQ
LSEASKITAQ KPTQRVIGLE PNQQEYRILV VDDRWENRQL LLKLLQPTGF QVKEASNGQE
AIEIWQSWQP HLIWMDMRMP VMNGYEATQQ IKSHIQGQAT VIVALTASTL EEEKAVILSA
GCDDFVRKPF REEVIFEKMA QYLGVNYIYE ELDSEDTSET VIIEKLTAAA LAIMPDEWLK
KLVESATLID EQRIAKLLSQ IPQEHQALAK AIEKEVDNFD FDRLMNLAQE AINL
//
