ID X7EN36_9RHOB Unreviewed; 727 AA.
AC X7EN36;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OCH239_01920 {ECO:0000313|EMBL:ETX16606.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX16606.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX16606.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX16606.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) 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};
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:ETX16606.1}.
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DR EMBL; JALZ01000001; ETX16606.1; -; Genomic_DNA.
DR AlphaFoldDB; X7EN36; -.
DR STRING; 1449350.OCH239_01920; -.
DR PATRIC; fig|1449350.3.peg.388; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000022447; 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; 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; 3.30.565.10; 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; 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 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000022447}.
FT DOMAIN 1..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 393..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 577..713
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 131..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 727 AA; 77551 MW; 23B49B55618B6997 CRC64;
MSSLDDIKQM FFLECDELLE ALNDGLADIE AALPAGELDP EVINAVFRTV HSIKGGAASF
GLDAIVRFSH SFETVLDLMR SNKLLPDAEN VRVLHRCADH LADLVAAGRA DAPTDPSASE
ALVRRLDAMT PGSAAKAPEP VAVPQAPVED EPADGEVPLT FAPLAIPLAF DIADAAPGPG
IFRIDVAPSA ELFATGNDPV HLFRELAGLG DLTVTAITDE VPTLAELDPL MPYLRWQLQL
ETVSPEADIR EVFDFVEMLA EVRITRIDAG GESAADEDAP QIPAGSRPDA REEEASAEGA
ETFGVAGAGD GAGAAQGRSG QAKSAKSTVR VDLDLVDSLI NIVGELVINQ SFLTQSFIEA
NVANRADIGS SLDEYKGLAL QIQESVMSLR AQSVKQLFQR MARIVRETSE VAGKQVVFET
EGEDTEIDKT VIERLIEPLT HILRNAIDHG LEPTAKRRET GKPEAGTVRL SAFHRSGRVL
IEVSDNGGGI DRARVFEIAV KKGLVSPDAQ MSDAETDRLI FLPGFSTKEA VTDLSGRGVG
MDVVRSAIQK LGGRVAIQSV PGKGTRFSIS LPLTLAVLDG MVVDVAGQTM VVPITAVVET
IRPDPSALHW IGASAHVIKV RDALVPLVDL GLAFGYRTEP TEANELVLLL IETEQGDRWA
LAVDRIIDQR QVVIKSLERN YGHVEGVAAA TILGDGKIAL IIDPEEIACM AEREQTPPAP
MLAAIGE
//
