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 27-MAR-2024, entry version 105. 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; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC 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.TM_0904; -. DR PaxDb; 243274-THEMA_00115; -. DR EnsemblBacteria; AAD35985; AAD35985; TM_0904. DR KEGG; tma:TM0904; -. DR eggNOG; COG1776; Bacteria. DR InParanoid; Q9X006; -. DR OrthoDB; 9812187at2; -. 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 CDD; cd17909; CheC_ClassI; 1. DR Gene3D; 3.40.1550.10; CheC-like; 1. DR InterPro; IPR007597; CheC. DR InterPro; IPR028976; CheC-like_sf. DR NCBIfam; NF041093; CheC_Thtogales; 1. DR PANTHER; PTHR43693; PROTEIN PHOSPHATASE CHEZ; 1. DR PANTHER; PTHR43693:SF1; PROTEIN PHOSPHATASE CHEZ; 1. DR Pfam; PF04509; CheC; 2. DR SUPFAM; SSF103039; CheC-like; 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 FT S-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 //