ID K9THW7_9CYAN Unreviewed; 945 AA.
AC K9THW7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Oscil6304_2370 {ECO:0000313|EMBL:AFY81998.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY81998.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY81998.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY81998.1,
RC ECO:0000313|Proteomes:UP000010367};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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; CP003607; AFY81998.1; -; Genomic_DNA.
DR AlphaFoldDB; K9THW7; -.
DR STRING; 56110.Oscil6304_2370; -.
DR KEGG; oac:Oscil6304_2370; -.
DR PATRIC; fig|56110.3.peg.2820; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR InParanoid; K9THW7; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000010367; Chromosome.
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; cd00731; CheA_reg; 1.
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:SF10; 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:AFY81998.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010367};
KW Transferase {ECO:0000313|EMBL:AFY81998.1}.
FT DOMAIN 2..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 387..642
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 644..786
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 824..941
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 274..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 874
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 945 AA; 105891 MW; 227C4EC1984BEA6E CRC64;
MDFNDIQELL GAFIAETDEF LQSLETQLLA MEQIETAEAR KSTIKEMFRA AHSIKGSALM
FGFQSLSTAA HRIEDCFAIL RDRQEDTPLS SHSITQLLQG VDLLKKLTAQ STALVREKQA
EDPKDFQGDL EAIARIKQEL EAECGGLKQP AEWMQKHPAN TQVIQTIFQQ DLPPIFNRLE
TELSQIQAET VEDSYRVFNE IYYQLSGLSG MLEVPELGEI AECLRAAVDT PNLSVEDLKI
LGWAIAQNLE TLREQVLQEL PIVLQPMDIP DSTPDVVISP VPSPPPLLPS DSPPSATPPE
PSLLPTPTPG ESGVKPTIRV ELDRLTELVD LVGELVINRT HLEVQETQLR AEVKRLRRHI
RDLNQFGVQL REEYDRLAGE KSHRGRNTAH PLGFDALEMD HYTEFHDTAR ETIETTQAIA
HSSAKIDEVA LNLDRSTDRL RRICDRLRSQ VMQLRVVSFS RAVDHLPRAI RDMSRTYNKD
VNLLLIGRDT KIDESLLHAL RDPLVHLVRN AFDHGIESPE DRKAAGKPPN GQIEIEARHQ
GGQTIITISD DGQGIDPETI RDRLVELNLV SEEQALELSL NELYDFLFWS GFSTQREVND
LSGRGVGLDI VRSNLRQVRG TVKVDSRLGR GTSFIIKLPL MLSISDALLV RIEHQTLALP
LDAVEEILHV NASEIQMAMY QPMLRWRDEY IRLVPLNDLL HYQESSHDLP SPIPVGEDYM
PVLVLSSSEG ILAIVVDRLV GQQELVVKPL PQPLSKPTGI LGCTILGDGE VVSILDVDDL
IGQLHPHIQK AVVIQNETQG RNHPLPPGTR TPVPLLPPLP SQPQILVIDD SYTIRQMLSL
TLTRSRYRVA QAKDGQDALE QLHHGLKCAL IIADIEMPRM DGFEFLAEVK ENPQFSHIPV
AMLTSRSGAK HRQRAMDLGA VQYFTKPYNE RQLLEAIAQL IGATL
//
