ID B4W054_9CYAN Unreviewed; 1122 AA.
AC B4W054;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_3497 {ECO:0000313|EMBL:EDX72425.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX72425.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX72425.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX72425.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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};
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DR EMBL; DS989864; EDX72425.1; -; Genomic_DNA.
DR RefSeq; WP_006104380.1; NZ_DS989864.1.
DR AlphaFoldDB; B4W054; -.
DR STRING; 118168.MC7420_3497; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000003835; 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; 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; 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; 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 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT DOMAIN 3..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 552..787
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 789..940
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1003..1120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 966..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1053
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1122 AA; 125190 MW; FECA081FC5D39D5F CRC64;
MNDPNIREQS YHYFLEEAPE LMGIIEQELL DLRTNFSVNK VHHLMRTTHT LKGAAASVEL
DTIKTVAHSL EDIFKTLFNP DVVIDAEVEA LLFEGYECLR LPLTAEVMGG KINEAEVLDR
TAAVFAKLQE KLGDCFDQQA NIPSSLELGF DVTQSIFEVG VSQRLDQITE ALASNDPSVM
ADTLRSQAEV LLGVAESMNL PGFAAIASSA IAALENYPDQ AEMITQIALA DFQAGQKAVL
DGDRTQGGQP SQSLQELAGV VDGDLEDAAP VAAPENVWEA DLSDSEVSEE LAASDTYAAD
SVYPDEEFSQ RPITDSADFQ LDATDLTPLL DIDINEYEDY SVSEPETEGV EEPDSADLLD
SVWGNISVSE STIEEDVPVE SESESEEVFP VFKTPAHNFQ DSIPESVPTP PVEAEEPLTD
YVLPSPRVQQ ESVPETQPQT VRVNIDHLEH LNYSVGELLT YQNRQSLQDE QLQSAVRLVL
TRLQQHQQLL DELQDWHDRQ LHRSQQKRMS LRGRKRREAI QEKPSLAWQN PQTTIPNYFD
PLELDSYNEP QLLIQSLMDD TAQLTEATES IEVFASQFNQ TFDKQRRLLT SIRDTLMEAR
LLPLGTLFRR FPRVLQQLEV THNKSVELYM DGTEVLVDKV VVQKLYDPLL HLIRNAFDHG
IESPEVRQES GKTRQGTIAI DAYHQNRYLV IEVRDDGQGL NFEKIRQRAV EQRLIDAEKA
RRLSPAELAE FLFEPGFSTA SGLSDLSGRG IGMDVVRSQV ESLQGSVTVY SQPYYGTTFR
LQIPLNLTIA KLLLMEAGGQ TYALLSDAIE QIIIPPPERL RCWDEGKVLR WGTGKDEQLI
PIFSLAEVLD YHIPQPKTLV LSSQRPLVEQ TAKMSVILIR CQNRLLGLEV NQLVGEQELV
IRPLGSMIAP PDYVYGGCIL ADGGLALVLD GTTLMQSIAD QQTAKSPPEF TADFQSSMVA
LTGSTSVASD RNQRQLSPSR PAALPAAPEP PPPTPTPRRS PQLVLIVDDS ITVRQSLTFT
LQKAGYQILQ AKDGYEAIEQ LQNHGEIQVV ICDIEMPRMN GFEFLKYRQQ EPELAKIPVL
ILTSRSSEKH RLIATELGAN DYITKPFLEP QLLETVQQFI NA
//
