ID D9S3A5_THEOJ Unreviewed; 655 AA.
AC D9S3A5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Toce_1121 {ECO:0000313|EMBL:ADL07882.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL07882.1, ECO:0000313|Proteomes:UP000000272};
RN [1] {ECO:0000313|EMBL:ADL07882.1, ECO:0000313|Proteomes:UP000000272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC {ECO:0000313|Proteomes:UP000000272};
RX PubMed=21304740;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP002131; ADL07882.1; -; Genomic_DNA.
DR RefSeq; WP_013275922.1; NC_014377.1.
DR AlphaFoldDB; D9S3A5; -.
DR STRING; 555079.Toce_1121; -.
DR KEGG; toc:Toce_1121; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_9; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000000272; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
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 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; PF07194; P2; 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:ADL07882.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000000272};
KW Transferase {ECO:0000313|EMBL:ADL07882.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 273..524
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 526..655
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 655 AA; 73915 MW; 2F14CB2A78D163C9 CRC64;
MDNRYLNVFL EEANEHIQNL NNGLLALESE PSQEILDEIF RSAHTLKGMA GTMGFNKISE
LTHEMEDLLH EIRNGSLSIT NTIIDVLLKC VDMLQEMTEQ ISKEGWEGET DIRPAIAEIK
KVMSNTSNDS KAADESEGKD DTGFNEFELR LMEEAANKNL KTWELHVELE ENCLLKSARA
FLVFKTLENL GEIIKTKPHI QDIEDEKFDK EFYIYIISSR SEEDLLNAVN SVSELKSVNV
REINLGNFQK KLTVARETSS VKESPKETNR IRNTSKTLRV DIERLDNLMN LVSELIIIKT
RLEELDNLTE QGQKRKEALE YLERITSNLH DAVMKVRMVP IENVFNRFPR VVRDLSRELN
KEVKLVIEGA ETELDRTVID EIGDPLIHLI RNALDHGIET PSERLKKGKP REGTLKLKAF
HDGNNVVIEV SDDGRGIDVE KVLKKAQEKN MVDKSQVKKL KEIEILSFLF ESGFSTSERV
TDISGRGVGL DVVKTKIESL GGSVEIKTAK DEGTTFSIRL PLTLAIIQAL MVQLGQEKYA
IPLSAIKEIV IIPNTELKKV HKHEVILLRG NVIPVLRLHE MLDIPDNCLK NENLTVVIVK
KGEKDVGLIV DSLLGEQEIV IKSLGNFLKN IRFIAGATIL GDGQVALILD INALI
//
