ID L8M4T4_9CYAN Unreviewed; 849 AA.
AC L8M4T4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Xen7305DRAFT_00030730 {ECO:0000313|EMBL:ELS03351.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS03351.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS03351.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS03351.1};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS03351.1}.
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DR EMBL; ALVZ01000166; ELS03351.1; -; Genomic_DNA.
DR RefSeq; WP_006509534.1; NZ_ALVZ01000166.1.
DR AlphaFoldDB; L8M4T4; -.
DR STRING; 102125.Xen7305DRAFT_00030730; -.
DR PATRIC; fig|102125.3.peg.2352; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR OrthoDB; 510512at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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:ELS03351.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Transferase {ECO:0000313|EMBL:ELS03351.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..569
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 594..707
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 714..830
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 247..308
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 643
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 763
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 849 AA; 95574 MW; AE9D8DDF4D3CF967 CRC64;
MNQFTSQYRS SLAKQLLSSF GLSLVTVGLA TLGINYLLIR SNLEKQVQQR AQSIVHGLEF
ATEGMIELGN TEVLRRIVQN YATLEAVEEI AIINPEEFTL AHSSSTQNNK IYRSPYPQLP
AVMRQAAHTG IEKNLHVVSP DGEEFLLYIL PFSSIFFETP GKRGLAIVSV DLREIQQNAI
RTFFKSTLTM AVGTCVILCV MGLLIHRIIL APLNRLHQSL GESKKTGLFS LPSAMPSNEI
GFLAATFDEV FRQLENHEQL EKEIKERRQA EIALGKALDI QKQREIELEQ AKQELAISHD
RLADYNQTLE HKVQQRTAEL AKSIKEASKA RKVAEQANQA KSTFLANMSH ELRTPMNAII
GYSEMLHEEA EDLGQEDFIP DLQKIHSAGK HLLSLINDIL DLSKIEAGRM ELYLESFEID
TLLEDVVATV QPLVEKNHNK LKLIVADDLP SIFADMTKVR QSLFNLLSNA SKFTENGTVT
LKIKRYLAQD EDWIQFQVHD TGIGMTKNQM ARLFKAFTQA DASTTRKYGG TGLGLTITQR
FCQMMGGDIY VESEVNHGTT FTIKLPVQVQ KATPVESATD SEEQTIPMMT YRNTILVIDD
DPTVHDLMAR FLTKEKFRVI TASSGEEGIR LAKSLEPDAI TLDVMMPDLD GWAVLAALKA
DVQTSHIPVI MITMVDNQNL GYALGAADYI MKPISKNNLK EVLGKYNSQA AFNKILIVED
DADTREILRR QLEDYSGIVL EAENGRQALD IIAQETPELI ISDLMMPEMD GFELFNQLRQ
NQNWSSIPII VLTSKELTLI EREKLQGRVK QVFRKGGSQR TILLQELHKL LLRAIKRKLS
RHIEKSVEE
//
