ID A0YL97_LYNSP Unreviewed; 980 AA.
AC A0YL97;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L8106_10121 {ECO:0000313|EMBL:EAW38372.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38372.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW38372.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2006) 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 -!- 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:EAW38372.1}.
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DR EMBL; AAVU01000005; EAW38372.1; -; Genomic_DNA.
DR RefSeq; WP_009783253.1; NZ_AAVU01000005.1.
DR AlphaFoldDB; A0YL97; -.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 441640at2; -.
DR Proteomes; UP000000737; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAW38372.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Transferase {ECO:0000313|EMBL:EAW38372.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 556..622
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 628..680
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 721..979
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 533..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 682..709
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 980 AA; 110604 MW; 580FD2728966BEA2 CRC64;
MENHYPLQTL RKKSLSKVYF SLRKKPLKKV ISKLVIASAI LAVGLISGTS YGLVRSIILT
SSQENALKEA QKASLEIDQW LTELRSQAES IANNSNVRSM NWSQAEPFLQ LELDRLPNYY
MLSLVNVDGS YYTTKAGFVE GQNLRDRLHF QKALAGETTV SQPIISRSTG VYQISVCSPI
WSISPLNRQS LSAEQTSIRT QSLQSLNLPD NSLQKNTVRG VLCASVSIEK ISRIVEKISN
IPQYSYAFVL DKDGIPIVHP DPQILQERKS FLANSNSSKA TLAQKMVNSQ EGIELIYLNN
SWVYIAYNPT QQANWSIGLV IPQDRLEVQL RPLNLLATVI GILLTLATIF AIWQVQLFEE
TREQAARETL VNQLTEQIRA SLDLNTLLQI TVQEVMRVLG LSWVGFSWYQ TEQKHLEIVC
SSSQLKFSRN FPQINTFIEK NFTNFLVSSP IASAEMISWD QLEKTQLSDA NKTDLKKAGI
SCYFALPIQV NSNQKGYLIG LSSAPISNEK AILKLLKTIR GQLIIAITQA NLYKQVKEKV
ELLNQTLDER LEAQAQLQQK MEMLDRSSNG IIIRDMGHKI TYWNQGAENI YGWKKAEVMD
KNIHSLLTTI FPTSQAEVME QLLQEGTWTG ELQHQTKDFQ NIVAFSRWTL QRDEQGNPYA
ILEINSDITE RKAAEIALAY SETKLREKAT QLEATLVELQ RTQAQVIQNE KMSSLGQLVA
GVAHEINNPV NFIYGNLTHA EEYMQDLVNL LHLYQDNYPD STPEIQDEIE VVDLEFIEED
FPKILKSMKN GAKRIEDIVV SLRNFSRMDE ADLKEVNIHE GIDSTLMILQ SRLNLMGSQT
QIEVIKNYGN LPLVECYPGR LNQVLMNLLI NAIDAIQEKY NQPSLSAAQG TVPTIEISTE
LLENNQVQIR IKDNGYGVSE SAQDHLFDPF FTTKPVGKGT GLGLSIGYQI ITEKHQGNLY
CNCKLEAGAE FIIEIPRKQG
//
