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Database: UniProt
Entry: A0A0V7ZR72_9CYAN
LinkDB: A0A0V7ZR72_9CYAN
Original site: A0A0V7ZR72_9CYAN 
ID   A0A0V7ZR72_9CYAN        Unreviewed;       605 AA.
AC   A0A0V7ZR72;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BC008_27370 {ECO:0000313|EMBL:KST66913.1}, BC008_28805
GN   {ECO:0000313|EMBL:KST67197.1};
OS   Mastigocoleus testarum BC008.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Mastigocoleus.
OX   NCBI_TaxID=371196 {ECO:0000313|EMBL:KST66913.1, ECO:0000313|Proteomes:UP000053372};
RN   [1] {ECO:0000313|EMBL:KST66913.1, ECO:0000313|Proteomes:UP000053372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC008 {ECO:0000313|EMBL:KST66913.1,
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:KST66913.1}.
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DR   EMBL; LMTZ01000092; KST66913.1; -; Genomic_DNA.
DR   EMBL; LMTZ01000090; KST67197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V7ZR72; -.
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   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        32..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          250..303
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          352..599
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          191..218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          302..343
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   605 AA;  68828 MW;  04047ABFB4AED8E9 CRC64;
     MNSQAENIFQ KNSYSWFQRI IDKTKIGHKI TIGYGITIGI AAMGITVGLF VGDVYWKQPA
     LKQQEISHRE SALLMQLKDS LLETKSQFIP YITNPHLLEN YSSYLLIHSD KIIAVLSELE
     NEISHENQGL QRQNLADLQN FIQKHKDTTQ TYRKKLVTTI NKFNIINSDN QTIDTRNSRN
     LLVNFLESLE ALQLEKDIQE LNKLIAFAED KKRAANTNLN LAIQLQADIT KYSILLSVAI
     AIFLAFFTTW LITYPLTAVT KVAQKVANES NFDLIVPVTT KDEVGLLASS FNQMIQTVSK
     YIHELELARQ TLEQRVEERT QELSQALQNL QQTQSQLIQT EKMSSLGQMV AGVAHEINNP
     VNFIYGNIRH VNSYVDDLLA LLKLYQEEHI DVSPKILEEI ENIDLEFVTD DLPKTLSSMK
     IGAQRIRDIV LSLRNFSRLD EAEAKAIDIH EGIESTLLLL NHQIKKGIEV VRQYGDLMLV
     ECYPAQLNQV FMNILNNGMD ALQEQPEEFS KQIRIQTEVL ETKVNKSVRI RIKDNGPGIP
     LNIQEKLFDP FFTTKPIGKG TGLGLSISYS IVKKHKGEIE VISEPGKGTE FIIMLPTLMN
     QENYL
//
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