ID A0YJV6_LYNSP Unreviewed; 1211 AA.
AC A0YJV6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L8106_15270 {ECO:0000313|EMBL:EAW38787.1};
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:EAW38787.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW38787.1, 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:EAW38787.1}.
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DR EMBL; AAVU01000003; EAW38787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0YJV6; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; IPR003018; GAF.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAW38787.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Transferase {ECO:0000313|EMBL:EAW38787.1}.
FT DOMAIN 218..264
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 340..417
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 418..472
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 473..543
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 546..599
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 946..1203
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..483
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1211 AA; 135463 MW; 1E5146A98F66F1A6 CRC64;
MGQQENLSLQ EIMGFQAGVT FDHLLKIAIH IAQAPVGYIS LIDASCQWLK SQVGLQAQTY
HYLDFCETVI SLHYPDNCFK SAKTLKKDQT SSPTETRSPS DAGLSSSSKN FAPIILEDLS
TNKQFPTHPL LKFNPAIRCY FGIPIQTKEG VLVGMLSIMD YEPRHLSPDS LQALEAIAEQ
VSVQMNLHRQ LIHAKGKLIK LENTIQKRSS IWDIVRQERD FVCNVLDTLS ALVIVLDPQG
KIIRFNRICE EISGYSAQEI EGKTPQEFGL SIYHSPVETD AFSSKSSTSP AEFPPYCESE
WIDLNRRTHL IGWSNKIIYN PDGSVEHLIA TGTDITMRRE SEKMLRLLER AIAASPSGIV
ISDAKAKDNP IIYCNPTFER ITGYSSSDIQ GRNCRFLQGN DTDPQAIETI RNSLREAKDC
LVTLKNYRKD GTPFWNELAI SPVRDTTGEV THFIGIQTDI SERKRAEEAL KTSEERYRLL
AENATDLISR HNSEGIYLYA SPACRKLLKY EPEELIGHSA YDFFHPEDVA SVRASHQTLL
AQGEISLVSY RIRRRNGEYI WFETTAHAVR DPQTGEVQEL VAVSRDITTR KKAEVSLLER
SHLSLLEAEV GKALGQGGTT ITILQACSDA IASHLSVTGV AIWTVNRSTH HLELQVTSGQ
CEVENCSDCP ERISHNCLCL NFALVVEGRQ VGMMEISSRR SLTEQVQNAL YWIANAIAVG
IDRVAALEEL HSRREGLLFR LASQIRDSLD LNTILAKAVS EIRSLLQVDQ CHFLWYLPTT
DPRSSFVITH QAQSSNLSQG LVDYPPDCVS WLSEKIEQHQ SVQINDSSQV DGLDGQTRSA
LHQVGVASML FLPLETRSGQ RGAIVCNHYQ NTHDWTVNDV ELLQAVVDQL AIAIDQAELY
AQTRAAALAA QTQAAQLSHA LLDLQEKEAK LIQSEKMSSL GQMVAGIAHE INNPVNFIYG
NLDYVRDYTQ DLLDVLRLYQ ESYPTSSPEI KEKIEEVDLE FISEDLPKII ASMEMGADRI
RQIVVSLRNF SRLDEAEMKP VDIHEGIDNT LLILHSRWKA KKVGSGVQII KNYANLPKVE
CYAGQLNQVF MNIISNAIDA LDNRPDPRQI TIDTELFEVK NPADRLNIPY VRVKIKDNGS
GVSTAVQNRL FDPFFTTKPV GKGTGLGLSI SYKIVVEKHG GSLKCLSEPG QGCEFWIEIP
VEPPPELRPR D
//
