ID A0A1J1LPB2_9CYAN Unreviewed; 2087 AA.
AC A0A1J1LPB2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-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=PL9214640415 {ECO:0000313|EMBL:CUR34408.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR34408.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CZDF01000171; CUR34408.1; -; Genomic_DNA.
DR RefSeq; WP_072720903.1; NZ_LN889812.1.
DR STRING; 671072.PL9214640415; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000184315; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 6.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; 8.
DR Pfam; PF18947; HAMP_2; 3.
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; 11.
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; 11.
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:CUR34408.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..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 934..986
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1026..1078
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1351..1584
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1700..1813
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1822..1938
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1968..2085
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1632..1658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1247..1341
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1634..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2018
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2087 AA; 227045 MW; 4F8CEEFC68B41839 CRC64;
MSTTQLAKVS DQLDEKQLLK TLVAVKKGDF SVRMPLDQTG IAGKVADTLN DIIELNQRMA
AELERISKVV GKEGQINQRA TLGSAGGSWE ASVNSVNTLI TDLVQPTSET ARVIRAVANG
DLSQKMALDI EDRPLKGEFL QTAKIVNTMV DQLSSFASEV TRVAREVGTE GKLGVQAEVQ
GVAGTWKDLT DNVNLMAGNL TGQVRNIAEV ATAIANGDLS KKITVDVKGE ILELKNTVNT
MVDQLNSFAS EVTRVAREVG TEGKLGVQAE VKGVAGTWKD LTDNVNLMAG NLTAQVRNIA
EVTTAVANGD LSKKITVDVK GEILELKNTI NTMVDQLNSF ASEVTRVARE VGTEGKLGVQ
AEVRGVAGTW KDLTDSVNSM AGNLTGQVRN IAEVATAIAN GDLSKKITVD VKGEILELKN
TVNIMVDQLN SFASEVTRVA REVGSEGKLG GQAEVRGVAG TWKDLTDSVN FMASSLTGQV
RNIAEVTTAV ANGDLSKKIT VDVKGEILEL KNTINTMVDQ LSSFASEVTR VAREVGTEGK
LGVQAEVRGV AGTWKDLTDN VNSMASNLTA QVRNIAEVAT AIANGDLSKK ITVQVKGEIL
ELKNTINIMV DQLSSFASEV TRVAREVGSE GKLGVQADVR GVAGTWKDLT DSVNFMAGSL
TAQVRNIAAV TTAVANGDLS KKITVDVKGE ILELKNTVNT MVDQLNSFAS EVTRVAREVG
SEGKLGVQAE VRGVAGTWKD LTDSVNFMAG SLTAQVRNIA EVTTAVANGD LSKKITVDVK
GEILELKNTI NTMVDQLNSF ASEVTRVARE VGTEGKLGVQ AYVKGVAGTW KDLTDNVNLM
AGNLTAQVRN IAEVATAIAN GDLSKKITVD VKGEILDLKN TINTMVDQLS SFASEVTRVA
REVGTEGKLG GQAEVRGVAG TWKDLTDNVN SMAGNLTAQV RGIARVVTAV ANGDLKRKLM
LEAKGEIETL ADTINEMIDT LATFADQVTT VAREVGIEGK LGGQAKVPGA SGTWRDLTDN
VNELAANLTT QVRAIAEVAT AVTKGDLTRS ISVEAQGEVA ILKDNINQMI ANLRETTQKN
TEQDWLKTNL AKFTRMLQGQ RDLETVSKLI LSELAPLVSA QHGVFYLMDS GDNQSYLKLL
STYAYRERKH LANRFQLGEG LVGQCALEKE RILITEVPEN YIKISSGLGE SNPLNAVVLP
VLFEGQVTAV IELASFRRFS EIHLMFFDQL TESIAIVLNT IAASMRTEEL LKQSTALAEE
LQSQQKELRE TNERLEQQAR SLKASEELLK SQQEELQQKN EELEEKARLL AEQNTEVERK
NGEIEQARRS LEEKAEQLAL TSKYKSEFLA NMSHELRTPL NSLLILARLL SENSDSNLSL
KQVEYAQTIH AAGTDLLGLI NDILDLAKIE SGTISVEIDQ ILFSELQNYI DRTFRQIAVD
KGLNFLVDFD SKLPKGIYTD PKRLQQILKN LLSNAFKFTE KGQVTLRVEL VTFGWSHEQN
TLNQADMVVA FSVIDTGIGV PPEKQRIIFE AFQQADGTTS RKYGGTGLGL SISREIAQIL
GGEIILTSTL GVGSNFTLYL PYHYQIQEIE ETSETRLTGP ISSPHFRERL RSTPAAFGSL
RSISLPSENL KIGEPETQKL QNNGNLTDSS AEEQSSLASA APTLAQKATQ AYARPQTEAQ
LSAGVKIRDD RELLQPGQRV LLIVDQDVAE ARLLLEVARQ QGFKGIVACS SDAGLTMARE
FKPSAILLSL QFPGVEGWTV LDRLKHEITT RHIPVYVISE EDAQHRSLQL GALSFLKKPI
NREILVEHIA KLKAFIGTSV KKLLMLEGNP EQRQSIIDII GNGDISISSF EAGEAALTTL
KAEPFDTVVV GWQLTDMNGI EWLEQLESEE NLSTIPIVFY HPQPLTKKQE TNLKNLANNI
TLKFAKSPES LLDLTALLLH RVPAELPEAK RQILEVLRQT DAILAGKKVL VVDDDVRNIY
AITSMLERHL MDVMYAENGK EAIAKLQATT GIDIVLMDVM MPEMDGYETM RAIRAVPKFE
SLPIIALTAK AMQGDREKCL DAGASDYITK PVDTEQLLSL LRVWLYR
//
