ID   CHEX_THEMA              Reviewed;         155 AA.
AC   Q9X1V3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=CheY-P phosphatase CheX;
DE            EC=3.-.-.-;
GN   Name=cheX; OrderedLocusNames=TM_1618;
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 [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   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), AND SUBUNIT.
RX   PubMed=15546616; DOI=10.1016/j.molcel.2004.10.018;
RA   Park S.-Y., Chao X., Gonzalez-Bonet G., Beel B.D., Bilwes A.M., Crane B.R.;
RT   "Structure and function of an unusual family of protein phosphatases: the
RT   bacterial chemotaxis proteins CheC and CheX.";
RL   Mol. Cell 16:563-574(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG   Midwest center for structural genomics (MCSG);
RT   "The crystal structure of the protein CheX from Thermotoga maritima.";
RL   Submitted (JAN-2005) to the PDB data bank.
CC   -!- FUNCTION: Involved in restoring normal CheY-P levels by
CC       dephosphorylating CheY-P. It has a greater activity than CheC.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15546616}.
CC   -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36685.1; -; Genomic_DNA.
DR   PIR; D72232; D72232.
DR   RefSeq; NP_229418.1; NC_000853.1.
DR   RefSeq; WP_004082082.1; NZ_CP011107.1.
DR   PDB; 1SQU; X-ray; 2.40 A; A/B=1-155.
DR   PDB; 1XKO; X-ray; 2.48 A; A/B=1-155.
DR   PDBsum; 1SQU; -.
DR   PDBsum; 1XKO; -.
DR   AlphaFoldDB; Q9X1V3; -.
DR   SMR; Q9X1V3; -.
DR   STRING; 243274.THEMA_06155; -.
DR   EnsemblBacteria; AAD36685; AAD36685; TM_1618.
DR   KEGG; tma:TM1618; -.
DR   eggNOG; COG1406; Bacteria.
DR   InParanoid; Q9X1V3; -.
DR   OMA; NVEYINP; -.
DR   OrthoDB; 1956590at2; -.
DR   EvolutionaryTrace; Q9X1V3; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1550.10; -; 1.
DR   InterPro; IPR028976; CheC-like_sf.
DR   InterPro; IPR038756; CheX-like.
DR   InterPro; IPR028051; CheX-like_dom.
DR   PANTHER; PTHR39452; PTHR39452; 1.
DR   Pfam; PF13690; CheX; 1.
DR   SUPFAM; SSF103039; SSF103039; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Hydrolase; Reference proteome.
FT   CHAIN           1..155
FT                   /note="CheY-P phosphatase CheX"
FT                   /id="PRO_0000250998"
FT   HELIX           3..19
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          40..51
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   HELIX           62..72
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   HELIX           83..105
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          130..141
FT                   /evidence="ECO:0007829|PDB:1SQU"
FT   STRAND          145..151
FT                   /evidence="ECO:0007829|PDB:1SQU"
SQ   SEQUENCE   155 AA;  16449 MW;  C5ED437A8400C37C CRC64;
     MDARIVNALI GSVYETIRDV LGIEPKTGKP STVSHIEIPH SLVTVIGITG GIEGSLIYSF
     SSETALKVVS AMMGGMEYNQ LDELALSAIG ELGNMTAGKL AMKLEHLGKH VDITPPTVVS
     GRDLKIKSFG VILKLPISVF SEEDFDLHLS VKSGG