ID G6G0F8_9CYAN Unreviewed; 1833 AA.
AC G6G0F8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=FJSC11DRAFT_4607 {ECO:0000313|EMBL:EHC08365.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC08365.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC08365.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC08365.1,
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:EHC08365.1}.
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DR EMBL; AGIZ01000022; EHC08365.1; -; Genomic_DNA.
DR RefSeq; WP_009460362.1; NZ_AGIZ01000022.1.
DR GeneID; 60768530; -.
DR PATRIC; fig|741277.3.peg.4165; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 10.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 5.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 9.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 10.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 4.
DR PROSITE; PS50885; HAMP; 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHC08365.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..66
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 106..158
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 198..250
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 290..342
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 382..434
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 474..526
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 566..618
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 658..710
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 750..802
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 842..894
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1167..1400
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1446..1559
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1568..1684
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1714..1831
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1403..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1060..1157
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1495
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1617
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1764
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC08365.1"
SQ SEQUENCE 1833 AA; 199898 MW; 19786152BB093A1E CRC64;
TWKDLTDSVN FMAGSLTAQV RNIAEVTTAV ANGDLSKKIT VDVKGEILEL KNTINTMVDQ
LNSFASEVTR VAREVGTEGK LGVQAEVRGV AGTWKDLTDS VNMMAGNLTG QVRNIAEVAT
AIANGDLSKK ITVDVKGEIL ELKNTINIMV DQLGSFASEV TRVAREVGSE GKLGVQADVR
GVAGTWKDLT DSVNFMAGSL TAQVRNIAEV TTAVANGDLS KKITVDVRGE ILELKNTINT
MVDQLNSFAG EVTRVAREVG AEGKLGVQAE VKGVAGTWKD LTDSVNFMAG SLTAQVRNIA
EVTTAVANGD LSKKITVDVR GEILELKNTI NTMVDQLSSF ASEVTRVARE VGTEGKLGVQ
AEVKGVAGTW KDLTGAVNMM AGNLTDQVRN IAEVATAIAN GDLSKKITVQ VKGEIFELKN
TINIMVDQLN SFASEVTRVA REVGSEGKLG VQADVKGVAG TWKDLTDSVN FMAGSLTAQV
RNIAAVTTAV ANGDLSKKIT VDVKGEILEL KDTINTMVDQ LNSFASEVTR VAREVGTEGK
LGVQAEVRGV AGTWKDLTDS VNSMAGSLTS QVRNIAEVTT AVANGDLSKK ITVDVKGEIL
ELKNTINTMV DQLNSFASEV TRVAREVGTE GKLGVQAYVR GVAGTWKDLT DNVNLMAGNL
TAQVRNIAEV TKAVANGDLS KKITVDVRGE ILELKNTINT MVDQLSSFAS EVTRVAREVG
TEGKLGGQAQ VQGVAGTWKD LTDNVNSMAS NLTAQVRGIA KVVTAVANGD LKRKLMLDAK
GEIEALAETI NEMIDTLATF ANQVTTVARE VGIEGKLGGQ AKVPGAAGTW KDLTDNVNEL
AATLTTQLRA IAEVATAVTK GDLTRSIAVE ALGEVAILKD NINQMIANLR ETTQKNTEQD
WLKTNLAKFT RMLQGQRDLE TVSKLILREL APLVGAAHGV FYIMENTDNS QYLKLLSSYA
YRERKHLANR FQLGEGLVGQ CALEKERILL TEVPHDYIKI SSGLGEATPV NVVVLPVLFE
GQITAVIELA SFRRFSEIHL TFFDQLTESI AIVLNTIAAS MRTEELLKQS QSLAEELQSQ
QNELRETNKR LEQQAQTLKA SEDLLKKQQE ELQKTNAELE EKAELLAVQN KEVERKNHEI
EQARLSLEEK AEQLALSSKY KSEFLANMSH ELRTPLNSLL ILAKILADNV EGNLSEKQIE
YSRTIYSAGN DLLSLINDIL DLAKIESGTM SIDMDQLRLT DLREQVERTF RQVAVDKRLN
FTIELDPELP PTIYTDAKRL QQILKNLLAN AFKFTEKGEV SLRVFVAKQG WSSDQENLNR
ADRVIAFAVK DTGIGIAPEK QKIIFEAFQQ ADGTTSRKFG GTGLGLSISR EITRLFGGEI
KLVSRPGEGS TFTLYLPQPL SGAGEMGRTG DGVKSSPHHP TTPPPHHTPI TPVIDDRNNI
QPGDRTLLIV EDDTKFARIL LDMVRQNEFK GIVAHSGNTG LALAQEYQPS AIILDIRLPG
MDGWAVLDRL KHDANTRHIP VHVMTVEEGK QRSLQQGAIA YLQKPISSET LHQALTKIKG
FVDRRVKNLL IVEDDENQRQ SIVALIGNGD VATTAVSTGN QALSAIANGK FDCVVLDLGL
PDMSGFELIE QIKKLPNGET LPIIVYTARE LTRSEDTQLQ RIAETVIVKD VRSPERLLDE
TALFLHRVQA NLPAPKRQIL EQLQNSDFQL AGKKVLIIDD DVRNIFALTS MLERYQMQIF
YAENGSDGIE VLQNNPDINV VLMDVMMPEM DGYETTRRIR ANPDFKSLPI IALTAKAMQG
DREKCIEAGA SDYITKPVDT EQLLSLLRVW LYR
//
