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
//