ID   CHEA_SALTY              Reviewed;         671 AA.
AC   P09384;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Chemotaxis protein CheA;
DE            EC=2.7.13.3;
GN   Name=cheA; OrderedLocusNames=STM1921;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3278311; DOI=10.1073/pnas.85.5.1403;
RA   Stock A., Chen T., Welsh D., Stock J.;
RT   "CheA protein, a central regulator of bacterial chemotaxis, belongs to a
RT   family of proteins that control gene expression in response to changing
RT   environmental conditions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1403-1407(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBUNIT: Trimer or tetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: May have three functional domains: one for interaction with
CC       CheB and CheY, a second for regulating phosphorylation and controlling
CC       the stability of the protein, and a third for receiving input signals
CC       regulating CheA activity.
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DR   EMBL; J03611; AAA27034.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20837.1; -; Genomic_DNA.
DR   PIR; A28959; A28959.
DR   RefSeq; NP_460878.1; NC_003197.2.
DR   RefSeq; WP_000061302.1; NC_003197.2.
DR   PDB; 1I5N; X-ray; 2.14 A; A/B/C/D=1-138.
DR   PDBsum; 1I5N; -.
DR   AlphaFoldDB; P09384; -.
DR   SMR; P09384; -.
DR   DIP; DIP-61270N; -.
DR   IntAct; P09384; 2.
DR   STRING; 99287.STM1921; -.
DR   PaxDb; P09384; -.
DR   EnsemblBacteria; AAL20837; AAL20837; STM1921.
DR   GeneID; 1253442; -.
DR   KEGG; stm:STM1921; -.
DR   PATRIC; fig|99287.12.peg.2038; -.
DR   HOGENOM; CLU_000650_3_6_6; -.
DR   OMA; MMDMAKS; -.
DR   PhylomeDB; P09384; -.
DR   BioCyc; SENT99287:STM1921-MON; -.
DR   BRENDA; 2.7.13.3; 5542.
DR   EvolutionaryTrace; P09384; -.
DR   Proteomes; UP000001014; 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; 3.30.70.400; -; 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; IPR015162; CheY-binding.
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; PF09078; CheY-binding; 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; 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_0000074710"
FT   DOMAIN          1..105
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   DOMAIN          274..526
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          528..663
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   REGION          256..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:1I5N"
FT   HELIX           9..29
FT                   /evidence="ECO:0007829|PDB:1I5N"
FT   HELIX           37..56
FT                   /evidence="ECO:0007829|PDB:1I5N"
FT   HELIX           60..77
FT                   /evidence="ECO:0007829|PDB:1I5N"
FT   HELIX           85..106
FT                   /evidence="ECO:0007829|PDB:1I5N"
FT   HELIX           113..130
FT                   /evidence="ECO:0007829|PDB:1I5N"
SQ   SEQUENCE   671 AA;  73013 MW;  07AFFC34FBA5DB01 CRC64;
     MSMDISDFYQ TFFDEADELL ADMEQHLLDL VPESPDAEQL NAIFRAAHSI KGGAGTFGFT
     ILQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKNSEE PDAASFEYIC
     NALRQLALEA KGETTPAVVE TAALSAAIQE ESVAETESPR DESKLRIVLS RLKANEVDLL
     EEELGNLATL TDVVKGADSL SATLDGSVAE DDIVAVLCFV IEADQIAFEK VVAAPVEKAQ
     EKTEVAPVAP PAVVAPAAKS AAHEHHAGRE KPARERESTS IRVAVEKVDQ LINLVGELVI
     TQSMLAQRSN ELDPVNHGDL ITSMGQLQRN ARDLQESVMS IRMMPMEYVF SRFPRLVRDL
     AGKLGKQVEL TLVGSSTELD KSLIERIIDP LTHLVRNSLD HGIEMPEKRL EAGKNVVGNL
     ILSAEHQGGN ICIEVTDDGA GLNRERILAK AMSQGMAVNE NMTDDEVGML IFAPGFSTAE
     QVTDVSGRGV GMDVVKRNIQ EMGGHVEIQS KQGSGTTIRI LLPLTLAILD GMSVRVAGEV
     FILPLNAVME SLQPREEDLH PLAGGERVLE VRGEYLPLVE LWKVFDVDGA KTEATQGIVV
     ILQSAGRRYA LLVDQLIGQH QVVVKNLESN YRKVPGISAA TILGDGSVAL IVDVSALQGL
     NREQRMAITA A