ID A0A0V7ZIK0_9CYAN Unreviewed; 591 AA.
AC A0A0V7ZIK0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BC008_16800 {ECO:0000313|EMBL:KST64296.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST64296.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST64296.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST64296.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
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:KST64296.1}.
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DR EMBL; LMTZ01000125; KST64296.1; -; Genomic_DNA.
DR RefSeq; WP_027846872.1; NZ_LMTZ01000125.1.
DR AlphaFoldDB; A0A0V7ZIK0; -.
DR OrthoDB; 479493at2; -.
DR Proteomes; UP000053372; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053372};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..306
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 344..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 201..228
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 294..335
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 591 AA; 67199 MW; 2FFCB8173B877D27 CRC64;
MKNNENAIPL SKQLNQWVGY LKVGHKIGLG YGLAIFVAIL GTTTGFVIGD SYHKEALERE
EASLNAYRLV NDLQNKALLI RLDWLELPII LDKPELVKKQ KAAIKEHQTE FKRLWVKFKS
KFNKTEEKEE EKQESIISEN YSARLIYESY SQFPDLYLQQ VEELIKNLNF NNIQPTKLET
TRTQLTNFSN TEYSRKLEYF AKDLLSLSQE MYEEYEKAEA EFAVAQQLRL KIFFASAVLS
VLIAILLATF TSRAISKPLQ SVTDVAQKTT QEANFDLQAP VTTSDETGKL ATSLNQLILR
VKQLLIEKEQ KSEELQKANE KLIMTQKQMV AQEKLASLGS LTAGIAHEIR NPLNFVNNFA
QLSVELVQEL SEEIAQQTTN INEDTAESIT DILSLLSTNV SKIEHHGQRA EKIVGNMLLH
ARNGGHLWES SNLNQLLEET ANLAYHGIRA KDSSFNVTFD TDYDENIGEI EVVIQDISRA
FLNILGNACY AIQQKLKQQG NEFTPILNIR TRNLQDKVEI RIRDNGSGMT PEVRDRIFEH
FFTTKPTGEG TGLGLSLTYD IIVQQHQGSL EVESEVDIYT EFIITLPKKN Q
//
