ID A0YVG7_LYNSP Unreviewed; 1016 AA.
AC A0YVG7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L8106_21634 {ECO:0000313|EMBL:EAW34955.1};
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:EAW34955.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW34955.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:EAW34955.1}.
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DR EMBL; AAVU01000036; EAW34955.1; -; Genomic_DNA.
DR RefSeq; WP_009786461.1; NZ_AAVU01000036.1.
DR AlphaFoldDB; A0YVG7; -.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9760752at2; -.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 2.
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; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAW34955.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 153..311
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 540..764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 789..904
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 318..345
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 838
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1016 AA; 115961 MW; DB67541B7AF2A282 CRC64;
MQDINFVYSE PIDLTNCDRE PIHIPGQIQP HGVLLTFQEI DLTILQASQN AIDFLGVEAQ
SLLGKKLNDI FVDADIQFIT QAVSQNIDFD YFNPFEIRPK NTSCYPQFEG VIHRIDDILC
LELELKSNSQ ISYPLSFYHL LKASLKSIVN VDDFQESTHQ LVREVSKITG YDRVMIYQFE
EDGSGVVIAE AKKKELESYL GLHYPTSDIP LQARKLYCQN WLRLIMDINY KPVDIVPVLN
PLNNQPLDLS NSVLRSVSPI HVEYLQNMGV AASLCISLIK DDQLWGMIVC HHYEAKYVNY
ETRKACEFLG QFMSIELFKK HYKELEKYQH KVSELQKEFK NILSIQPANI NNFLQNNGDR
LLSLVNASGI LIALEDELIV FGNTPPTNAV KKLLYWLKNN HQVELFKTNN ISEYYPDFYP
YKKNASGILV ISIFSMNTSY QIVWLRPERT QTVTWAGNPS KPVTLAKDGT MQLSPRRSFE
VWKQTIQGCS LPWKKIELDA ALELRNILML TALQSSQLAL EQVAQRAEIA NQAKSEFLAN
MSHEIRTPMN AILGFCDLLQ GLVTEPRQRS YLELIAASGE SLLDLINDIL DLSKIEAGKF
QLYYEPLNLR QLIAEVQKIF THRAKEKGLS LISHIDDAVP QGIYFDGIRL RQILFNVLGN
AIKFTERGFI QISIRAQVYT QENIKKVWLE IAITDTGIGI AKNQQDDIFE AFVQSEGQST
RKYGGTGLGL AITRRLTTLL GGTLVLQSEL SHGSSFIFIF PEIEVSDISL ESEIASLVDE
DLNQFYNSTI LAIDDVYSNL QLIQGYFEGT QHHLLLAQNG ESAIQLAKTE QPDVILLDWL
MPNMDGRGVF NALKQNEKTQ NIPIFIITAS VLRQDYLDVQ LLCQGVLHKP TNRAQLVSAL
KTVLPSTKCQ STITSETSLS QVNKTEDIQQ LPQLLETLNQ EKIIWEQLRI TLKKREVKEF
AQRLQTYGTN HKCQILLDYT QELFTQLEAF DWQNIPKTIE HFLIILQQIN NQNNEF
//
