ID CHEA_THEMA Reviewed; 671 AA.
AC Q56310;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=TM_0702;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8550470; DOI=10.1128/jb.178.2.484-489.1996;
RA Swanson R.V., Sanna M.G., Simon M.I.;
RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium
RT Thermotoga maritima.";
RL J. Bacteriol. 178:484-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 293-671.
RX PubMed=9989504; DOI=10.1016/s0092-8674(00)80966-6;
RA Bilwes A.M., Alex L.A., Crane B.R., Simon M.I.;
RT "Structure of CheA, a signal-transducing histidine kinase.";
RL Cell 96:131-141(1999).
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 Q56310; Q56311: cheW; NbExp=3; IntAct=EBI-1039701, EBI-15580256;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; U30501; AAA96387.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35784.1; -; Genomic_DNA.
DR PIR; D72346; D72346.
DR RefSeq; NP_228511.1; NC_000853.1.
DR RefSeq; WP_004081040.1; NZ_CP011107.1.
DR PDB; 1B3Q; X-ray; 2.60 A; A/B=293-671.
DR PDB; 1I58; X-ray; 1.60 A; A/B=352-540.
DR PDB; 1I59; X-ray; 1.80 A; A/B=352-540.
DR PDB; 1I5A; X-ray; 1.90 A; A/B=352-540.
DR PDB; 1I5B; X-ray; 1.94 A; A/B=352-540.
DR PDB; 1I5C; X-ray; 1.90 A; A/B=352-540.
DR PDB; 1I5D; X-ray; 2.90 A; A=350-540.
DR PDB; 1TQG; X-ray; 0.98 A; A=4-104.
DR PDB; 1U0S; X-ray; 1.90 A; A=175-260.
DR PDB; 2CH4; X-ray; 3.50 A; A/B=355-671.
DR PDB; 2LD6; NMR; -; A=1-131.
DR PDB; 3JA6; EM; 12.70 A; C/E=293-671.
DR PDB; 3UR1; X-ray; 4.50 A; A=355-671.
DR PDB; 4JPB; X-ray; 3.19 A; A=355-671.
DR PDB; 4XIV; X-ray; 3.00 A; A/B=289-540.
DR PDB; 6MI6; X-ray; 2.95 A; A/B/C/D=353-539.
DR PDBsum; 1B3Q; -.
DR PDBsum; 1I58; -.
DR PDBsum; 1I59; -.
DR PDBsum; 1I5A; -.
DR PDBsum; 1I5B; -.
DR PDBsum; 1I5C; -.
DR PDBsum; 1I5D; -.
DR PDBsum; 1TQG; -.
DR PDBsum; 1U0S; -.
DR PDBsum; 2CH4; -.
DR PDBsum; 2LD6; -.
DR PDBsum; 3JA6; -.
DR PDBsum; 3UR1; -.
DR PDBsum; 4JPB; -.
DR PDBsum; 4XIV; -.
DR PDBsum; 6MI6; -.
DR AlphaFoldDB; Q56310; -.
DR BMRB; Q56310; -.
DR SMR; Q56310; -.
DR DIP; DIP-29071N; -.
DR IntAct; Q56310; 3.
DR STRING; 243274.TM_0702; -.
DR DrugBank; DB02524; 2',3'-O-{4-[Hydroxy(oxido)-Lambda5-azanylidene]-2,6-dinitro-2,5-cyclohexadiene-1,1-diyl}adenosine 5'-(tetrahydrogen triphosphate).
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR PaxDb; 243274-THEMA_01155; -.
DR DNASU; 898369; -.
DR EnsemblBacteria; AAD35784; AAD35784; TM_0702.
DR KEGG; tma:TM0702; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR InParanoid; Q56310; -.
DR OrthoDB; 9803176at2; -.
DR BRENDA; 2.7.13.3; 6331.
DR EvolutionaryTrace; Q56310; -.
DR Proteomes; UP000008183; 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:0019904; F:protein domain specific binding; IPI:CAFA.
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:SF1; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chemotaxis; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..671
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000074718"
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 291..541
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 543..671
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 304
FT /note="D -> G (in Ref. 1; AAA96387)"
FT /evidence="ECO:0000305"
FT HELIX 4..29
FT /evidence="ECO:0007829|PDB:1TQG"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:1TQG"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:1TQG"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:1TQG"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:2LD6"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1U0S"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:1U0S"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1U0S"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1U0S"
FT STRAND 225..237
FT /evidence="ECO:0007829|PDB:1U0S"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:1U0S"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1U0S"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:1U0S"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 300..322
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4XIV"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 393..413
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 428..439
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:1I58"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:2CH4"
FT HELIX 493..498
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1I58"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:1I58"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 530..538
FT /evidence="ECO:0007829|PDB:1I58"
FT STRAND 542..551
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:4JPB"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 588..594
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 620..637
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 648..655
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:1B3Q"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:1B3Q"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:1B3Q"
SQ SEQUENCE 671 AA; 75556 MW; F264398B88DA34E1 CRC64;
MMEEYLGVFV DETKEYLQNL NDTLLELEKN PEDMELINEA FRALHTLKGM AGTMGFSSMA
KLCHTLENIL DKARNSEIKI TSDLLDKIFA GVDMITRMVD KIVSEGSDDI GENIDVFSDT
IKSFASSGKE KPSEIKNETE TKGEEEHKGE STSNEEVVVL PEEVAHVLQE ARNKGFKTFY
IKVILKEGTQ LKSARIYLVF HKLEELKCEV VRTIPSVEEI EEEKFENEVE LFVISPVDLE
KLSEALSSIA DIERVIIKEV TAVTEESGAE KRTEKEEKTE KTEEKAERKK VISQTVRVDI
EKLDNLMDLM GELVIARSRI LETLKKYNIK ELDESLSHLS RITLDLQNVV MKIRMVPISF
VFNRFPRMVR DLAKKMNKEV NFIMRGEDTE LDRTFVEEIG EPLLHLLRNA IDHGIEPKEE
RIAKGKPPIG TLILSARHEG NNVVIEVEDD GRGIDKEKII RKAIEKGLID ESKAATLSDQ
EILNFLFVPG FSTKEKVSEV SGRGVGMDVV KNVVESLNGS ISIESEKDKG TKVTIRLPLT
LAIIQALLVK VNNLVYAIPI ANIDTILSIS KEDIQRVQDR DVIVIRGEVI PVYRLWEVLQ
IEHKEELEEM EAVIVRVGNR KYGIVVDDLL GQDDIVIKSL GKVFSEVKEF SGAAILGDGS
IALIINVSGI V
//
