ID A0A2T1D3M6_9CYAN Unreviewed; 1174 AA.
AC A0A2T1D3M6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7B76_14440 {ECO:0000313|EMBL:PSB15125.1};
OS filamentous cyanobacterium CCP2.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB15125.1, ECO:0000313|Proteomes:UP000239512};
RN [1] {ECO:0000313|EMBL:PSB15125.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB15125.1,
RC ECO:0000313|Proteomes:UP000239512};
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|EMBL:PSB15125.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB15125.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Keele B.F.;
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 -!- 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:PSB15125.1}.
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DR EMBL; PVWD01000093; PSB15125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1D3M6; -.
DR Proteomes; UP000239512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000239512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 55..276
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 337..381
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 422..471
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 550..605
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 791..1023
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1054..1172
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 764..791
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1103
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1174 AA; 130711 MW; 2C4982963C50086D CRC64;
MILVTLLFSH YAAITAQARD QLRFDNAVQR TQATIQNRLD TYIALLYAGR GLFAASDRVT
QQDFQTFVNQ LQLQQRYPGI QGIGFSARVL SNELDSFLTE MRSQGLENFS VRPQAPPRDE
YHTIVYLEPM DRRNRAAIGY DMFTEPRRRA AMERARDTGV HAASSKVILV QEIDIDKQAG
FLIYVPIYRT GEVPSTVAER REALEGFIYS PFRADDFLEG VLGNERERRI DIQVYDGTEL
QAEKLLHRSK DATSTASPHF IHIAPMDVGG QPWSLVFTSR PEFEASLDRN QVPYILLSGL
GLAAVLFAMT RSQNRARIAA EQTAISLQRS EAALREREAR LRCLVDANII GVVVGDQQGQ
ILEANDAFLN IVGCSREELL SGYMNWANIT SLEQPNSAES RIEGQPIEEQ PIEGMLPLRN
QDPFQKEYIR KDGTRIPVMV GTAVLDEPGN LGVGFIIDLT KQKRAEKAVQ QSEIRFRTLI
EQSPLSTQIF SPNGKTVQVN RAWENLWGLS LDLLGEYNIL QDQQLVDLGI MPYVQKGFAG
EATIIPSVQY DPKQAIPGKP TCGGPQRWVQ AFIYPVKDEV GNIREVVLLH EDITERKLAE
QALQNTNDRL GLLYSMSSSL LLHEQPKDFI TSLFNQLSRH LQLEVYLCYL FDREQNILQL
HAFGGLPEAL VHQIEWIALG QSVCGKVAQE QQPMVVESVQ QNTEPIVEHI RSLGITAYAC
YPLLSHGQLI GTLSFGTRNR PNFSGDELAL MQVVSEQVAT ALERSRLIAE LQQQTKELSQ
ANQAKDEFLA TLSHELRTPL NAILGWTQLL RTRKFDEKTT NRALETIDRN TKSLAQLIED
ILDVSRIITG KLRLNLSNVP LIPVIEAAID TIRAAAEAKN IQITTQLDPE VDTVIGDENR
LQQIVWNLLS NAVKFTPDGG QIEIWLEQIE IKETPKGKKL QDTFSRARIS VSDTGRGISP
DFLPHVFDRF RQADSSTTRT FGGLGLGLAI VRHLVELQGG TVYAESPGEG QGTTFSVELP
LLTDRISLSA PKQTASTPQD KPSFIKQHPL NGVQILVIDD EIDTRELIAT VLQQAGANVT
TVANANQALA ALPQLKPDVL VSDIGMPDMD GYTLIRQIRT MPAEQGGTIP AIALTAYAGI
WDQQQALSAG FQLHLSKPIE PEAFVEAIST LVSS
//
