ID A0A2P8WKX3_9CYAN Unreviewed; 751 AA.
AC A0A2P8WKX3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7271_01995 {ECO:0000313|EMBL:PSN20464.1};
OS filamentous cyanobacterium CCP5.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN20464.1, ECO:0000313|Proteomes:UP000240885};
RN [1] {ECO:0000313|EMBL:PSN20464.1, ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|EMBL:PSN20464.1,
RC ECO:0000313|Proteomes:UP000240885};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA Moore K., Momper L.;
RL Submitted (MAR-2018) 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 -!- 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:PSN20464.1}.
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DR EMBL; PYEQ01000016; PSN20464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8WKX3; -.
DR OrthoDB; 436952at2; -.
DR Proteomes; UP000240885; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
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; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000240885}.
FT DOMAIN 24..70
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 96..147
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 255..302
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 514..748
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 751 AA; 84157 MW; C83CF0F9F7FE0376 CRC64;
MNHQQSKPFS EPFFRTDGFT ADEASSLLTQ ILNGVADPIF IKDTQHLWRF VNRAFCDLFG
YDAKLLLGKS EQEFWPLEAT RCLEIEQAVF ETGQEQTYES VLCDANGSEH VVVIKIEPLS
GMGESAWVVG TVLDVTQQRQ SEEKLRQQAE RERILGAIAQ HLIQSLSSEQ MLERAVEAIC
RFLRADRVLF LSCDPDYQGI LAEATEPGIT PYVGSTVGSS LESLGLSSDR LSAYHLGQFQ
IIPGLAAEPA TDAALESLRV KACLVIPVIQ AESLYGLITV HHGQVREWQT WEIDTLQEVA
AQIGSALNQT RLYKQVSQLN AALEQQIDQR SEELRTALQF EATLKRITDR VRDSLDEKQI
MLTAVREVTE ALEAKGSNTS LYDLEQGTSK IYYEYNRSLP SYQGRVALME AFPEVYNQLL
QGQYFQFCSK EPNPARGRVS MLACPILDDR GVLGDLWLIN DESYGFNEIE IRLVQQVANQ
CAIAIRQAHL YKAAQIQVEE LERLNQLKDD FLSTVSHELR TPVTSMRVAL QLLGVTLNRE
LDLDGELQKS KPEQAPVARY YQILKEECER EISLINDLLD LQRLDVGNHP VNPEPVVLGD
WLPTLVNGFT PRTRNRDQSL DLNLPVEDLV IHTDLASLER ILAELLNNAC KYTPPGETIR
LEVTELVEAG DTLVQFQLAN TGVEIPETEM TRIFDKFYRV PSADPWKQGG TGLGLALVEK
LVLYIGGKIA VDSGDGQTCF TITLPRQLAA A
//
