CHEC_THEMA
ID CHEC_THEMA Reviewed; 205 AA.
AC Q9X006;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=CheY-P phosphatase CheC;
DE EC=3.-.-.-;
GN Name=cheC; OrderedLocusNames=TM_0904;
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 (1.75 ANGSTROMS), AND MUTAGENESIS OF GLU-13; ASN-16;
RP GLU-112 AND ASN-115.
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 (2.5 ANGSTROMS) IN COMPLEX WITH CHED.
RX PubMed=16469702; DOI=10.1016/j.cell.2005.11.046;
RA Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W.,
RA Bilwes A.M., Crane B.R.;
RT "A receptor-modifying deamidase in complex with a signaling phosphatase
RT reveals reciprocal regulation.";
RL Cell 124:561-571(2006).
CC -!- FUNCTION: Involved in restoring normal CheY-P levels by
CC dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a
CC structural motif that mimics a CheD substrate recognition site to bait
CC and inactivate it.
CC -!- SUBUNIT: Heterodimer with CheD. The CheC-CheD heterodimer interacts
CC with phosphorylated CheY. The CheC-CheD dimer has higher phosphatase
CC activity than CheC alone. {ECO:0000269|PubMed:16469702}.
CC -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD35985.1; -; Genomic_DNA.
DR PIR; G72318; G72318.
DR RefSeq; NP_228712.1; NC_000853.1.
DR RefSeq; WP_004080665.1; NZ_CP011107.1.
DR PDB; 1XKR; X-ray; 1.75 A; A=1-205.
DR PDB; 2F9Z; X-ray; 2.40 A; A/B=1-205.
DR PDBsum; 1XKR; -.
DR PDBsum; 2F9Z; -.
DR AlphaFoldDB; Q9X006; -.
DR SMR; Q9X006; -.
DR STRING; 243274.THEMA_00115; -.
DR EnsemblBacteria; AAD35985; AAD35985; TM_0904.
DR KEGG; tma:TM0904; -.
DR eggNOG; COG1776; Bacteria.
DR InParanoid; Q9X006; -.
DR OMA; LYIETEI; -.
DR OrthoDB; 1755994at2; -.
DR EvolutionaryTrace; Q9X006; -.
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; IPR007597; CheC.
DR InterPro; IPR028976; CheC-like_sf.
DR Pfam; PF04509; CheC; 2.
DR SUPFAM; SSF103039; SSF103039; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Hydrolase; Reference proteome.
FT CHAIN 1..205
FT /note="CheY-P phosphatase CheC"
FT /id="PRO_0000250997"
FT MUTAGEN 13
FT /note="E->S: Loss of activity, in absence of CheD; in
FT presence of CheD, activity greater than wild-type CheC
FT alone. Loss of activity, in absence of CheD; when
FT associated with S-112. In presence of CheD, reduced
FT activity but exceeds activity of CheC alone; when
FT associated with S-112."
FT /evidence="ECO:0000269|PubMed:15546616"
FT MUTAGEN 16
FT /note="N->S: Loss of activity, in absence of CheD; in
FT presence of CheD, activity greater than wild-type CheC
FT alone. Loss of activity, in absence of CheD; when
FT associated with S-115. In presence of CheD, almost no
FT activity; when associated with S-115."
FT /evidence="ECO:0000269|PubMed:15546616"
FT MUTAGEN 112
FT /note="E->S: Loss of activity, in absence of CheD; in
FT presence of CheD, activity greater than wild-type CheC
FT alone. Loss of activity, in absence of CheD; when
FT associated with S-13. In presence of CheD, reduced activity
FT but exceeds activity of CheC alone; when associated with S-
FT 13."
FT /evidence="ECO:0000269|PubMed:15546616"
FT MUTAGEN 115
FT /note="N->S: Loss of activity, in absence of CheD; in
FT presence of CheD, reduced activity. Loss of activity, in
FT absence of CheD; when associated with S-16. In presence of
FT CheD, almost no activity; when associated with S-16."
FT /evidence="ECO:0000269|PubMed:15546616"
FT HELIX 5..30
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1XKR"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 59..71
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1XKR"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:1XKR"
FT HELIX 104..129
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1XKR"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1XKR"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:1XKR"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:1XKR"
SQ SEQUENCE 205 AA; 22549 MW; 0FF88D0E26A927B7 CRC64;
MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI FIAKDPEEIV
VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL NLDEFSASAL REIGNIMCGT
YVSALADFLG FKIDTLPPQL VIDMISAIFA EASIEELEDN SEDQIVFVET LLKVEEEEEP
LTSYMMMIPK PGYLVKIFER MGIQE
