CHEA_LISMO
ID CHEA_LISMO Reviewed; 618 AA.
AC Q48768;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=lmo0692;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=12067;
RX PubMed=7803815; DOI=10.3109/10425179409020856;
RA Dons L., Olsen J.E., Rasmussen O.F.;
RT "Characterization of two putative Listeria monocytogenes genes encoding
RT polypeptides homologous to the sensor protein CheA and the response
RT regulator CheY of chemotaxis.";
RL DNA Seq. 4:301-311(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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 (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; X76170; CAA53765.1; -; Genomic_DNA.
DR EMBL; AL591976; CAC98770.1; -; Genomic_DNA.
DR PIR; AD1161; AD1161.
DR RefSeq; NP_464219.1; NC_003210.1.
DR RefSeq; WP_003733164.1; NZ_CP023861.1.
DR AlphaFoldDB; Q48768; -.
DR SMR; Q48768; -.
DR STRING; 169963.lmo0692; -.
DR PaxDb; Q48768; -.
DR EnsemblBacteria; CAC98770; CAC98770; CAC98770.
DR GeneID; 985032; -.
DR KEGG; lmo:lmo0692; -.
DR PATRIC; fig|169963.11.peg.713; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_9; -.
DR OMA; MMDMAKS; -.
DR PhylomeDB; Q48768; -.
DR BioCyc; LMON169963:LMO0692-MON; -.
DR BRENDA; 2.7.13.3; 3045.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.1110; -; 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 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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55052; SSF55052; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chemotaxis; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..618
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000074715"
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 233..488
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 490..618
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT MOD_RES 45
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 132
FT /note="T -> A (in Ref. 1; CAA53765)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> Q (in Ref. 1; CAA53765)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="D -> E (in Ref. 1; CAA53765)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> E (in Ref. 1; CAA53765)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> V (in Ref. 1; CAA53765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 68628 MW; 63B560C05D8E941C CRC64;
MTTNMLDLFI EEASEHLQAL NDNLLQLEKD PTNGQLVSEI FRSAHTFKGM SATMGFQQVA
DLTHAMENVL DEVRNNRLAV TEHLVDIIFT CTSHLETMVS DIQHGGQGAA DISKTVADLE
ALLHPEQETD LTVEKTYRIA IQIEEAAILK AVRAVMCLER LAEMGIISET TPDREAIELE
EFEQSFEVVL ESAQTKDEIK AVILDISEIE KVTVTEEVEE VQVIEPIKKA AKQTTKRLEN
KTIRVQLEKI EKLMNVFEES VIERARIDEI AEKTNNKELM EHLGRFSSIS KEIQNGLLNM
RMVPVDSVFN RFPKMVRTLA KELGKKIDLV IEGADTEVDK IVIDEIGDPL VHLIRNSVDH
GAETVEVRRK NGKNETATIN LKAFHSGNNV VIEIADDGAG INKRKVLEKA IAKNVVTRAE
STKMTDAEIF DLLFDSGFST ADQVSDLSGR GVGLDVVRNT ILKIGGKISV ESSENAGSTF
RIEIPLTLSI IQSMLVATSE RRYAVPLANV AEAITINPAD IQHVHGKDLI NYRETIIEVL
DLGECFHETP LNDTDELLLL VVKNAKRTFG LIIKDIIGQR EIVLKTLGGF FSESQIAFSG
ATILGDGRVV LILNLETF
