ID K9ST40_9SYNE Unreviewed; 1059 AA.
AC K9ST40;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Syn7502_01001 {ECO:0000313|EMBL:AFY73116.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY73116.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY73116.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY73116.1,
RC ECO:0000313|Proteomes:UP000010385};
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 Synechococcus sp. PCC 7502.";
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; CP003594; AFY73116.1; -; Genomic_DNA.
DR AlphaFoldDB; K9ST40; -.
DR STRING; 1173263.Syn7502_01001; -.
DR KEGG; synp:Syn7502_01001; -.
DR PATRIC; fig|1173263.3.peg.1031; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_10_3; -.
DR OrthoDB; 581426at2; -.
DR Proteomes; UP000010385; 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; cd00130; PAS; 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; 2.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF13426; PAS_9; 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; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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};
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:UP000010385};
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 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 386..438
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 461..502
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 536..588
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 606..820
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 846..962
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 430..464
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 895
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1059 AA; 119043 MW; DCDEB46B42AB5C9A CRC64;
MNNSKANLKT NLQAKFKQPK IKVPLLFILA VPFISQVLLA MGVVSYLSIK NGQESIKDIA
QQLGQSLGDR IDQNLENYLS IPKQINQTNL NAVKLKLLDI KNLKTWEKYL WQQVQIYPTV
NFISVGNYKG EYRTGERLAD GSFRINVVDP VKITQLGKKT INRNFYSFKT NALGDRTTGS
LIMENFDPTK WSFYQKAVAA GKTTWSDPYI SLLEPTLLIS AVTPIYEQNQ PVGVINTALR
LDGIGSYLRN LKVGGSGQAF IMDKNGILIA TSTAELPFRV QGGQGRELFK AVNSTNALTK
AVANAVDSYG NSQSNTMGQM QLNFDQKAYF LQVIPVTNNL GLNWLTVVII PESDFMEQIE
ANRNNLILVY VITAIAISIV AWFTSRWISF PILKIVNASR EIADGNLDAK ISPQRIKELD
LLAHSYNYMS EQLQNSFADL GEALDNLELK VEQRTWQLQR AERKYRSMFE NSVEGIFQTT
PAGYYINANP ALVKILGYDS REDLMVSLQD LNHNLYVLPN RRHEFEQLIS QYGEVNDFES
RVYRKDRSII WISETARMVK DSDNEILFYE GTVQDITTRK AIEGELQTAI QTAETANQAK
SAFLANMSHE LRTPLNAILG FTQVLIRDRS LNAEQQENLN IISRSGEHLL NLINDVLDMS
KIEAGKMTLQ EDNFNLKEML DSLVQMMRLR AETKNLELIC DYGIIPHYVI ADERKLRQVL
LNLLSNAVKF TEAGSITLQV DQDQDFLHFA VQDTGLGIAI AEQERLFTAF SQTASSHAQE
GTGLGLAISQ KLVQLMHGHI SVTSQVGVGS RFEFSIPLKI GNALEVEANL PQSQIIGLEP
NQPVYRILSV DDRLENRKLI TKLLTPLGFE VKEASNGQEA IDLWATWSPH LICMDMRMPI
MDGYAATEYI KSHLKGQATI IIALTASVLE EERVIVMSSG CDDFIRKPFR EETLLTKIAA
HLGVKYAYSN ANPESQEQVI PTERLTSREI ADLMPETWIT NLKLAAQAGD DEAIMQLIGE
ISSESTEYTD LRYKLMELIE NFNFEAIANL ASSINLNKS
//
