ID G6FZN0_9CYAN Unreviewed; 754 AA.
AC G6FZN0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FJSC11DRAFT_4329 {ECO:0000313|EMBL:EHC08665.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC08665.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC08665.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC08665.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) 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:EHC08665.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGIZ01000017; EHC08665.1; -; Genomic_DNA.
DR RefSeq; WP_009459929.1; NZ_AGIZ01000017.1.
DR AlphaFoldDB; G6FZN0; -.
DR GeneID; 60768266; -.
DR PATRIC; fig|741277.3.peg.3843; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EHC08665.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW Transferase {ECO:0000313|EMBL:EHC08665.1}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 207..258
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 255..326
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 328..380
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 393..617
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 636..752
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 120..147
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 687
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 754 AA; 83886 MW; 0439FC416D2C3591 CRC64;
MPEQPIKVLL VEDNPGDVRL LQEFLWDVTT AQFELMPVER LDRTLKLLNQ ESFDVILLDL
SLPDSQGLET FITLHRQAPA IPIIVLTGLD DENLALRAMQ EGAQDYLVKG QVSGDLLVRC
MRYAIERQRI EEALRQSEER FRVALKNSPI VVFNQDKELR YTWVYNTSPG FINEEILGKR
DLDLTAAADA QLVFDIKQRV LSTGIGIRKE VSITTAQGIR YFDLTVEPLR NEAQEVIGVT
CASIDISDRK LAEEKIREQA ALLDVTTDAI FVRDLDNRVI LWNKGAENLY GWLVQEAYGK
KVVELLYDDE PPEEVEIALL TVINQGKWQG ELPRVTKSGK KVLVSSRWSL VCQEDGTPKS
ILTVDTDITE KKQLETQLFR AQRLESIGTL ASGIAHDLNN ILTPILAVSQ LLPLKFPNIY
SEHEHLLEIL EDSARRGADL VKQVLSFARG VEGKRMTLQV KHLIREVVKI IKQTFPRSIE
VCIDVAPDLW TVYGDSTQLH QVLMNLCVNA RDAMPDGGSL TISAENLLID ENYARMNLDA
KVGPYTVVTV ADTGVGIPRE IVERIFEPFF TTKELGKGTG LGLSTVIGIV KSHGGFVNVY
SEVGRGTQFK VYLPAAQKIQ IESTPQLEPL AGKEELILVV DDEPAIQEIT RASLETHNYK
TLVASDGIEA IALYAQNRDK ISAVLMDIML PSLDGLTAIR TLQKINPSVK IVATSGLASS
SKLAQASTTN ISGFISKPYT VKELLLTLQK VLNG
//