ID A0A2S6CZM0_9CYAN Unreviewed; 967 AA.
AC A0A2S6CZM0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CUN59_00715 {ECO:0000313|EMBL:PPJ65205.1};
OS Cuspidothrix issatschenkoi CHARLIE-1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Cuspidothrix.
OX NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ65205.1, ECO:0000313|Proteomes:UP000239589};
RN [1] {ECO:0000313|EMBL:PPJ65205.1, ECO:0000313|Proteomes:UP000239589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ65205.1,
RC ECO:0000313|Proteomes:UP000239589};
RA Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT cyanobacterium.";
RL Submitted (FEB-2018) 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:PPJ65205.1}.
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DR EMBL; PGEM01000004; PPJ65205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CZM0; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000239589; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
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; 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; 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; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 2.
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; 2.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PPJ65205.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000239589};
KW Transferase {ECO:0000313|EMBL:PPJ65205.1}.
FT DOMAIN 1..110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 204..311
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 440..688
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 690..824
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 848..964
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 251
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 897
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 967 AA; 107913 MW; A23E9E24982E8DE1 CRC64;
MSKYTLFDLF VEEVKTSIGT LKRCLPVLKN QPFSQDEIEQ AIQATHSLYG TAYIMEMEAA
YNLVQLMKDC LIAVQKQSIT LKIEHIDILI HASDLLLSMS LVAEDNLDVW MKNHLGDWNN
TQQAIAYLIT GNLPNELLLN LEKTEVTQPK EIIDNTAFVT DEKEEKIANI NQISPITDFE
PHPVISTSPV ISAPMPPTIE PPVMSGDSGS MMDLFRLEAE AQVNVLNNGL LIIENNPQSA
QELEALMRAA HSIKGAARIV ELDQVVQLAH VMEDCFVAAQ KKTVSLTPDD VDILLQGVDL
LQNISQLNDA ELPTWLGQHQ GNFINLRDDV AAILSPGSKK PKTNTTPNIE KDVQIVDHSP
IANVQPLVTK SASPITTREE DNTNSTKNQD RVVRVSADNL NRIMGLAGES LIEANWLQPF
ADSMMLLKSR MLEIARSLEQ LQESLDQNLY ETEGKEYLLQ ARQQKQECID YISDNLNELE
LYVRRTGSLS DRLYREVINS HMRPFEDGLH SFPRMIRDLA RKLNKQVKLE IVGKSTPVDR
DILKKLEAPL THILRNAVDH GMELPEERIS TGKPPEGIIR LEAFHRGGML AITISDDGKG
VNREQLRQKI INKNLATADM ATQLSDAELM EFLFLPGFST AKQVTEISGR GVGLDIAKSM
AQEVGGTVRA NSHPGKGTSF HFQLPLTLSV VRTLLVEISE NSYAIPLARI DQIVTLDRAE
ITNVENRQYF TMNNQNIGLI AAYQILELPL SKQQNDSVSV VVISDQNSSY GLVVDKFLGE
RDLVVRPLDP RLGKVADISA TALLGDGSPI LIVDVSDMVR SMDAILKTRN LSKVMMQAEL
ESIHQQPKIL VVDDSITVRE MERKLLENRG YLVDTAVNGV EGWNAVRTNN YNLVISDIDM
PKMNGIELVK QIKSNPRLNS LPIIIISYRD REEDRLQGLE AGADYYLTKS SFHDDTLINA
VVDLIGN
//
