ID A0YVS3_LYNSP Unreviewed; 1161 AA.
AC A0YVS3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L8106_18332 {ECO:0000313|EMBL:EAW34838.1};
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:EAW34838.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW34838.1, 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:EAW34838.1}.
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DR EMBL; AAVU01000038; EAW34838.1; -; Genomic_DNA.
DR RefSeq; WP_009786566.1; NZ_AAVU01000038.1.
DR AlphaFoldDB; A0YVS3; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR OrthoDB; 414909at2; -.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17569; REC_HupR-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00065; GAF; 2.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 532..746
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 805..921
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 971..1111
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 854
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1161 AA; 130824 MW; E0AAABB5EB753AB0 CRC64;
MNFLKKSKPK ILVVDDEPDN LDLLYRTFYR AYKVLRADSA PQALEILAQE EDVAVIISDQ
RMPQMSGTEL LSVAATQYPD AIRILLTGYT DVEDLVEAIN SGQVFKYVTK PWEAEELKVI
VNQALETHNV LKTRTEELKR ALQQESLLNA VTSTIRSALN YREMLQRIVE TVGQMFEVSY
CILQPFQDGE MVEEWFVYQA SRLKESDFGI ENSEFKTLVW ETTEVDIIPD AQTDERIQGE
SEEFLARKQA YTAANICSSL IVPLFYQQEL MAVLAMHQVD DLREWLNHEV QLIITVADQA
ALALSQARAY EQVQELAKRE VLVNTITAAI RSSLDPQKIF AAITQQLGQA LSVDGCALSL
WTREDEFVQC VGLYDAHYET SVVGDWSEDE IDAVDPIDET SADAKSPENL PQSAVPIRGN
PVLQRLLDTQ NPVVINDLTK KPDWNLIELP LRSPSKALMV VPLLLDDQII GSISLRQNDS
IRKWTEAEVN LVQVVAAQAA LAVQQARLYQ KTRQQAERLL EVDRLKTEFF QNISHEFRTP
LTLMIGPLEA AVNQTQDLPY EQAKIALRNS RRLLRLVNQL LDLQRFDAGR MQPSFRPCDL
VEFCRQTVES FQPYCEKKGI KLEISLQLCE SIYLDLERFD KVLYNLLSNA MKFTPENGVI
YISLEPSGSY CRLQVKDTGI GIHREQIPHL FERFRQAEGS TNRSYEGSGL GLALVKELVD
LHHGQVSVDS VYGEGTTFTV WLQTGTAHLP ADQVLEVPAE LNPRRAAVEL SDVEVELSED
EVSNPTEESL VDEHLIATSE PLENTILVVD DNPDLRRYLS NILKPAKFHV VMARNGAEGF
EQAKTYRPEV IITDLMMPVV SGLDLIRMIR EDVQLRGTPI ILLTAKADED TRIEGVERGA
DAYVSKPFND RELLAEVRNL RALKENERRV AELNRYLTES VLKRFLPPPM VERAAAGDLV
LDLNPEPRLV TILFTDIVGF TRMSNQLQSR RIAQVLNEYL AAMTQAVFEN GGTVDKFIGD
AVMALYGAPQ ELPPDEQVRR ALASARAMLR ALDKLNLSWQ ERSLVGHNGV EPIRFRCGIH
QGMAVVGMFG SKERSDYTAI GPSVNIAARL QEVACPNHIL VSAEVAQYLD QREILSEEMQ
SLKGIDEPVS TFMIASEPIA E
//
