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CHEA_THEMA
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   25-MAY-2022, entry version 164.
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; Thermotogae; Thermotogales; Thermotogaceae; 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.THEMA_01155; -.
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   DNASU; 898369; -.
DR   EnsemblBacteria; AAD35784; AAD35784; TM_0702.
DR   KEGG; tma:TM0702; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   InParanoid; Q56310; -.
DR   OMA; NELVECC; -.
DR   OrthoDB; 305000at2; -.
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; 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   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
 
 
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