ID G2J2F9_PSEUL Unreviewed; 722 AA.
AC G2J2F9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:BAK76335.1};
GN OrderedLocusNames=NH8B_1513 {ECO:0000313|EMBL:BAK76335.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76335.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK76335.1; -; Genomic_DNA.
DR RefSeq; WP_014086714.1; NC_016002.1.
DR AlphaFoldDB; G2J2F9; -.
DR STRING; 748280.NH8B_1513; -.
DR KEGG; pse:NH8B_1513; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_4; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000001274; 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; 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 Kinase {ECO:0000313|EMBL:BAK76335.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW Transferase {ECO:0000313|EMBL:BAK76335.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 300..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 572..710
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 722 AA; 77896 MW; 644CF1AB08E7EF93 CRC64;
MDELLTVFVT ESREQLAALE AALLQLEEAS GDADTLHAIF RAAHTIKGGA GVIECDYIVA
FTHVVENVLD QLRNGDIAVS AELIALLLAC GDHIGLLLGE FESGRVHPTA ELQLAGDALL
ARLQRDAQTA PPGLPPAEAS SATQPGLGRD LIESECWHIS LRFERHVLKN GMDPLSFLHY
LGTLGTIVHL ETVADAMPPA DQMDAEACYL GFEIRFASCA DKTTIERVFE FVRDDCTLHI
LPPDSRLADY IDLLQSLPED TMRLGEILVR IGALTQAELD DGLLMQQPPM AGAAPPDVVP
LGEILVQQQV VQPKLVEAAI IRQAQVNDKK TAEARLIRIQ ADKLDRLIDL VGELVIASAS
VSLLASRTGR AELLEASSLM MRLVESTRDS ALQLRMVQIG ETFSRFNRIV RDVSKELGKD
IELVITGGET ELDKSVVEKI GDPLIHLVRN AIDHGIEPTA HRAAAGKPPR GRLELNASHD
SGSIVITVSD DGGGLNRDKI VAKATERGLL QPGHNLSEAE IDNLIFEPGF STADHVSNLS
GRGVGMDVVK RNIQSLRGHV DVRSAPGAGT RFSIRLPLTM AIIDGFLVGT GQANYVVPLD
MVVECLELSP QTSDNHYLNL RGEVLPFIRL HELFNLPGKR PARENVVVVR TGAQKVGIVV
DQLLGEFQTV IKPLGHLFQS LRGIGGSTIL GSGEVALILD VPALVAIATR RESREAASTS
AT
//
