ID K9RTV2_SYNP3 Unreviewed; 1026 AA.
AC K9RTV2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Syn6312_1376 {ECO:0000313|EMBL:AFY60547.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY60547.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
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};
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DR EMBL; CP003558; AFY60547.1; -; Genomic_DNA.
DR RefSeq; WP_015124091.1; NC_019680.1.
DR AlphaFoldDB; K9RTV2; -.
DR STRING; 195253.Syn6312_1376; -.
DR KEGG; syne:Syn6312_1376; -.
DR PATRIC; fig|195253.3.peg.1390; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000010379; 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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
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; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFY60547.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010379};
KW Transferase {ECO:0000313|EMBL:AFY60547.1}.
FT DOMAIN 11..114
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 496..730
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 732..874
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 901..1018
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 350..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..450
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 951
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1026 AA; 113706 MW; 1BFEE731B2CF5A59 CRC64;
MVPPKSQLIP ANDGQEIVRQ QFLEEAQDYL EAMETGLLGL SQDGQNRGRV DGILRAAHSI
KGGAAMMGFT QLSDLAHRLE DFLKVIRAGT PVEIDLEQQL LRGVDCLQHL ISLNRQGMIA
PQSWLDTQVD PVIEQLQARL GDLQPESEIA LLSEDAGGDM RALLFESEVE GCLQRLEAVL
ASPEQPCLLE ELKIVAQELE GLGQMLELPA FVSYCASVSD LLEHQPYPLA AIATEIVQGW
RRCQAMVLVG QFQALPERFI SWSKTTDFID LEELPELSDL ELDAEALFAP DAVPDYPALE
PLDISHDQPE ATLPFREVGP KPALAGLENL LADVETALDD QEFDPVLEFS PSLLPDHAHP
TLPPTSASTI PSREPAPSAP AASESAGHAE AYKTVRVAVQ QLDELADLFG ELTIERNGLG
LHVQRLQQQM QALKDKVRRL EQSNFQLRQG YDRVTTQTFG IPTANLQQKL AKSEIAPHWQ
DQFDALEFDR YNPLHQLSQD VIETIVQIQE ITSDLEIGLE DTERTQRDLH RTAKQMQNRL
TQVRMRPFAD LANRYPRMVR DLCHEYGKGV QLEINGGNTL VDRTILEALT DPLLHLVRNA
FDHGIESPAE RTAQGKPNPA KITISAAYRG SQTIIQIADD GQGINLEKIK QRGLEMGLDA
MMLNQASERE LVDLIFEPGF TTAPQVTELS GRGVGMDVVR TNLKKIRGEI QVETKPGLGT
TFTITVPFTL SVVRVLLVEI AGMLVAVPTD AVEEMTLFEA ENLLHSAGQT LLDWDGLLMP
LIQLEQWFNF PRPRPRISME AAPIIDQPTL LVIAQGDHLL GIPTERYWGE QEVTIRQVDS
ALPLPPGFSG CTILGDGRIV PLVDTYGLWR WLETQQSQAP NLKPKSPGLV SSQPRQSRQT
TVLIVDDSIN VRRFLANTLE KAGYRVEQAK DGQEALDLLS NGLSAQAVIC DIEMPRLDGY
GFLSQAKNLK NQENLPVVML TSRSSEKHRQ LAINLGATAY FTKPFREADL LATLKTLVTS
PQPQPV
//
