Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Flagellar motor switch phosphatase FliY |
Protein Synonyms/Alias | |
Gene Name | fliY |
Gene Synonyms/Alias | cheD; OrderedLocusNames=BSU16320 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | 251 | EPVTPEPRIEPKQQQ | R | HTP | [1] | |
Reference | [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [ PMID:22517742] |
Functional Description From UniProt | FUNCTION: Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P |
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| Cellmembrane; Chemotaxis; Completeproteome; Flagellarrotation; Hydrolase; Membrane; Referenceproteome |
Protein Sequence | MENNRLSQDE IDALLNGTGS TLDEPEIPEV DDLSEMERDA IGEIGNISFG SSATALSTLL 60 NQKVDITTPS VTVIPRSKIS DAFPEPYVAI EVNYTEGFSG SNLLVVEQSD AAIIADLMIG 120 GDGKGADPSL GEIHLSAVQE AMNQMMGSAA TSMSTVFSKK IDISPPRVEL LDVTEEKGTD 180 RIPDDEMLVK VSFNLKVGEL IDSSIMQLYP LTFAKDLISS LMNSESAEEE ETVQPEVTYE 240 QPKEPVTPEP RIEPKQQQQP PKRQGTAKKA APVQVSPVEF SAFDPNEAVQ APIHNLDMLL 300 DIPLSITVEL GRTKRSVKEI LELSAGSIIE LDKLAGEPVD ILVNQRIVAK GEVVVIEENF 360 GVRVTDILSQ AERINNLK 378 |
| GO:0009425 C:bacterial-type flagellum basal body IEA:InterPro GO:0005886 C:plasma membrane IEA:UniProtKB-SubCell GO:0003774 F:motor activity IEA:InterPro GO:0004721 F:phosphoprotein phosphatase activity IDA:CACAO GO:0006935 P:chemotaxis IEA:UniProtKB-KW GO:0001539 P:cilium or flagellum-dependent cell motility IEA:UniProtKB-KW GO:0016311 P:dephosphorylation IDA:GOC |
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