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Database: UniProt
Entry: P74137_SYNY3
LinkDB: P74137_SYNY3
Original site: P74137_SYNY3 
ID   P74137_SYNY3            Unreviewed;       674 AA.
AC   P74137;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=sll1871 {ECO:0000313|EMBL:BAA18223.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA18223.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA18223.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18223.1; -; Genomic_DNA.
DR   PIR; S75662; S75662.
DR   AlphaFoldDB; P74137; -.
DR   IntAct; P74137; 1.
DR   STRING; 1148.gene:10499096; -.
DR   PaxDb; 1148-1653308; -.
DR   EnsemblBacteria; BAA18223; BAA18223; BAA18223.
DR   KEGG; syn:sll1871; -.
DR   eggNOG; COG2205; Bacteria.
DR   InParanoid; P74137; -.
DR   PhylomeDB; P74137; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016020; C: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; cd18773; PDC1_HK_sensor; 1.
DR   CDD; cd18774; PDC2_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; 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   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAA18223.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..383
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          444..666
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          375..434
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   674 AA;  74935 MW;  1322B0AACAA7D420 CRC64;
     MVSIIKSVRR SLLLKFVLSY FCLSSVVVAS IFLVANYRAV KGIESQTFNR LNISNNLKEY
     QLEQWMEGQK DTLFLLSDIN SIQANTELLK NTSVSDPQYK IIQKRLIEEL REIDLFLPHI
     EAINILNTGG IVVASNNLDE IGVYKGIGNQ TTYFANINSN FKTVPNFYFS KVYNRPSMTF
     ATNIKHDITR ERLGYLSIDI NLNAVDDLIR KRTGLGDTGE TFLVGEINNQ VSFIASDENK
     KLTANGSKPN FNSLGINSVM AGNSGQGSYV NYAGTPVLGV YQWIEKYNLA LITEISEVEA
     LELARRFTRM LVLVGLVSTA LLLIAVYLLS IKITKPILLI TKAAIDISSG DREARAPVLG
     EDELGILAKS FNLMTNELRE SNSSLEKKNQ ELELAQKQLA VANSCLEEKV QQRTEELENT
     VKALELASSE AEAANATKSI FLANMSHELR TPLNAIIGYS EMLIEEAEDL DSEELVPDLD
     KILRSGKSLL ALINDLLDIS KIEAGKMELY LETFNLKELI AGILDTISPL LKNNNNKLEV
     EISLESEEVY GDLIKLRQGI LNLLSNASKF TKDGIISFIV EEFKVDEKDW LSFQVKDTGI
     GLTEEQMSKL FQPFTQADSS TTRKYGGTGL GLAITRKFCQ MMGGDIYLTS EIGVGSSFTI
     KLPKYAQLNS AKND
//
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