ID L8N5Z8_9CYAN Unreviewed; 2107 AA.
AC L8N5Z8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Pse7429DRAFT_0225 {ECO:0000313|EMBL:ELS34559.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS34559.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS34559.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS34559.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS34559.1}.
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DR EMBL; ALWB01000007; ELS34559.1; -; Genomic_DNA.
DR RefSeq; WP_009625279.1; NZ_ALWB01000007.1.
DR PATRIC; fig|927668.3.peg.351; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELS34559.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:ELS34559.1}.
FT DOMAIN 3..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1575..1814
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1815..1959
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1983..2100
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 696..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2033
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2107 AA; 233227 MW; AE27894224EAE91F CRC64;
MNSEQQQQRI MGYFIEEARE HLQTIEQGVL NLQEILDDSE SINELFRAAH SIKGGAAMLG
VGSIQHVAHR LEDFFKILKE NSQINVDERL KSLLLAGFDP LSELLEELQG GYKISDELTA
ETNNRVKPVF AELEAYLNQL VTEVDGEIST QTPAQTSSQK VPEKAVATIE QPDIVSQKSI
FQKEVTTKMR DMLQLFRSAD TPESRSQLQT VCNYFQEVGN NFDLRNWTNL VIQIKNAIAQ
PNNSYRTLAP ILIRELKEAQ DLVLDNREAE IVVSSQIQNL LPYRFSEPED DEVSTIFTTA
SGDIGFDNEP IAEDKSITDH DNIALDLNPI DIDLFADDAS EVNEEIFDLS EVNESQIDQI
DWMDGEYEIA ENQHIDGPKV GASELKSLAI LFENDDIDFD AAWEDIESNE TNMSNQGVTS
ASENRDDFAD LLGNASSNDD ETIPNLNNKE SSIDQLFGDF STEDSAAEIR AEESDDSLFP
SEDSLFPDDL DGVLNQVTDN FSELETDVDA EDAQTSQASI EELFSNDFGK ATDLDEQFDM
DLGLDLLEEN YNPQIENNLS NSDRIDQIDQ IDQIDQIDQI NQIDQIDQFD PFDDINISEI
NTDDIDFYDL SESSAEQLDD LSDSYLSDHN PIIDAQDESD SLSSEEYFAE IARQENAIAN
GNNDGSMEPF ALTFSEEGMT LLEDPFAIDE NLDGFLLGDS ASESPQEAKS ESNDADPLDT
TGLKIFDELG FDSDELDESV TFKEDVRIHD SSTSMDEETN EDLGGFFAGI SDLDDTNQAI
TNLSEATDDI DLIGEDGLEN FFDGISIDSP DNNNAINTDA TDDISSEDGL EEFFDGISTD
SADAINTDAT DDISSEDGLE EFFIESANNA DHNEISSLSD AIDEFSELDS DDNLDDFFAA
NNSFDSSLAT DPLVDDVSTD EPAQDLGDRI EDNFSQLDQS EQLDDDFFVN SELSSESISS
ESISAESIDD LGDITVDHDE QEFSINGDPD EFLDRSEQIE NITFTSKELS YEDDLAEEIS
DAESLADFFA ESESPAIASS HNINDEINDE INDELDDRHL ASYSENITNT DDLGDFFDVA
EDPQDLNKQE FVNFGESEDV NLDFLDMVTD EEVPAESSVD LAIEPFSEEL LSEELLSEEL
LAEESLTDNS DLADLFVNAG EEDLTVLESD FEFDGNGELT QSDEFADLTS VLDGALDGAL
DSALDSALDK EFQDFELESI EANLTTQEDI DLEVDSPSTA TTTIDNLVDF FQGNDEIEDN
SLSIEEIVSS DLAIDESIVF DESDPLSDLN QDDLGVDDSF TQDTQTKPTL ETENQLPPEE
LNGIDDNFDF DDLEAMIGSS INVADEGLNS EQTQQFSSSI NSINSNSTSQ VAPSVNVPRN
HQDVVNPDND DMDFDALEAL LGDADTIDAE TNAANNFTSI PPVPSKPPDD FDELENMLQS
AFAKDVGPIK TKAPVRPPTT TRKQRLTDTT MRVDVKYLDS LNNLVGELVV NRNLLEQDQE
RLQQFITNLL HQVQLLSDVS QRMRDQYDRS LLEASLTAGR GRSYSSFETS YANDGANSNS
SVSNDFEGIE FDRYNTFHVL SQEIIELIVR VRESASDIEF VVGETDQVTR QLGTITTQVQ
DDLKQSRMVP FAQIADRLPR GIRDRALKTG KQAELEIFGR ETLIDKAILE SLTDPLTHLV
NNAIDHGLED PATRQAAGKS ATGRLTVRAY HQGNQTVISI SDDGAGISPD RVKKSAVSKG
VRSQAEVDRL NDTEVYALLF EAGFSTAAQA DEFKGRGVGL DVVKTCLDDI RGVIIVESVI
GKGTTFTIRL PLTLSISKAM FCISDRARIA FPVDGFEDMV EVPQSQIVLN EKGQPCLPWR
DTILPFQHLS NLLSYSRHLS RSSIYGKQEN DELCIIILRN DTSYLALQVD QFLGEYEIVI
KQLEGPIPQP AGIAGATVLG DGRVMAIANV LELFDIASGR LRPSTSGAPI QPTVEEDVAV
DPTVLIVDDS ITVRELLSLT FAKVGYRVEQ AKDGQDAWEK LRAGLPCDMI FCDIEMPRMD
GLDLLSRLQK DSRLKEIPVA MLTSRGADRH RQSAIQLGAK GYFTKPYLEE ELLSASKRLL
NGETLPI
//
