CHEA_RHIME
ID CHEA_RHIME Reviewed; 758 AA.
AC Q52880;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=R00639; ORFNames=SMc03007;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RU11/001;
RX PubMed=7623670; DOI=10.1111/j.1365-2958.1995.tb02274.x;
RA Greck M., Platzer J., Sourjik V., Schmitt R.;
RT "Analysis of a chemotaxis operon in Rhizobium meliloti.";
RL Mol. Microbiol. 15:989-1000(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(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 -!- INTERACTION:
CC Q52880; Q52879: cheY1; Xeno; NbExp=2; IntAct=EBI-6403466, EBI-6417929;
CC Q52880; Q52884: cheY2; Xeno; NbExp=6; IntAct=EBI-6403466, EBI-6403471;
CC Q52880; Q52878: orf2; Xeno; NbExp=5; IntAct=EBI-6403466, EBI-6417877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; U13166; AAA86674.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45211.1; -; Genomic_DNA.
DR PIR; S61834; S61834.
DR RefSeq; NP_384745.1; NC_003047.1.
DR RefSeq; WP_003529948.1; NC_003047.1.
DR AlphaFoldDB; Q52880; -.
DR SMR; Q52880; -.
DR IntAct; Q52880; 3.
DR STRING; 266834.SMc03007; -.
DR EnsemblBacteria; CAC45211; CAC45211; SMc03007.
DR GeneID; 61602106; -.
DR KEGG; sme:SMc03007; -.
DR PATRIC; fig|266834.11.peg.2012; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_5; -.
DR OMA; MMDMAKS; -.
DR BRENDA; 2.7.13.3; 5347.
DR Proteomes; UP000001976; 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 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 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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chemotaxis; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..758
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000074716"
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 367..607
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 609..745
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT REGION 293..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 189
FT /note="D -> E (in Ref. 1; AAA86674)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> A (in Ref. 1; AAA86674)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="N -> D (in Ref. 1; AAA86674)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="E -> K (in Ref. 1; AAA86674)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> P (in Ref. 1; AAA86674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 81102 MW; 9F03A8F24EA25D5D CRC64;
MDMNEIKEIF FQECEEQLAE LESGLLKLND GDRDPETVNA VFRAVHSIKG GAGAFGLDDL
VSFAHVFETT LDCVRSNRLE PNQDVLKVML RSADVLADLT NAARDGGGVD EARSRQLIKE
LEALANGELP QAAAESAPKT TPAGVAPAAP VVNEEGFQPV AFSFDDFETG DEPTIEPSTY
EIVFKPKSDL YSKGNDATLL LRDLSRLGEM SIHCNMDTLP PLDRMNPEEA YFSWKISLKT
DKGEEAIRSV FEFAEWDCEL DVALAGGTVG MDEDLPMQPV PFDLSILEDE AQAPAGEEDR
AAASEGDSRN AAVAAAQTAS NVLQMAQSTA RVSPENARNS QSASAAQAAA QQAASAATPT
IRVDLDRVDR LINLVGELVI NQAMLSQSVI ENDTNGTSSI NMGLEELQQL TREIQDSVMA
IRAQPVKPVF QRMSRIVREI ADMTGKSVRL ITEGENTEVD KTVIDKLAEP LTHMIRNAVD
HGLETPEKRV AAGKNPEGTV RLTAKHRSGR IVIELADDGA GINREKVRQK AIDNDLIAAD
ANLSDEEVDN LIFHAGFSTA DKISDISGRG VGMDVVKRSI QALGGRINIS SKPGQGSIFT
MSLPLTLAVL DGMVVTVANQ TLVVPLTAIV ETLQPEASAI HSFGSSQRLI SIRDSFCPLV
DVGRILNFRG AQANPVEGVA LLVESEGGGQ RALMVDAIQG QRQVVIKSLE ANYTHVPGIA
AATILGDGRV ALILDVDAIV AASRGQSLKP EMSLAAAG
