| Tag | Content |
|---|
| CPLM ID | CPLM-005231 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Sensor protein PhoQ |
Protein Synonyms/Alias | |
Gene Name | phoQ |
Gene Synonyms/Alias | b1129; JW1115 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 280 | TDLTHSLKTPLAVLQ | acetylation | [1] |
|
Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Member of the two-component regulatory system PhoQ/PhoP involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In presence of low periplasmic Mg(2+) concentrations, PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, which results in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In presence of high periplasmic Mg(2+) concentrations, acts as a protein phosphatase that dephosphorylates phospho-PhoP, which results in the repression of PhoP-activated genes and may lead to expression of some PhoP- repressed genes (By similarity). Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two- component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes. |
Sequence Annotation | DOMAIN 215 266 HAMP.
DOMAIN 274 480 Histidine kinase.
NP_BIND 385 393 ATP.
NP_BIND 415 420 ATP.
NP_BIND 434 446 ATP.
METAL 151 151 Divalent metal cation.
METAL 152 152 Divalent metal cation.
METAL 385 385 Magnesium.
METAL 442 442 Magnesium.
MOD_RES 277 277 Phosphohistidine; by autocatalysis (By |
Keyword | 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; Transmembrane; Transmembrane helix; Two-component regulatory system. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 486 AA |
Protein Sequence | MKKLLRLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY 60
TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR DVPWLMKMIQ PDWLKSNGFH 120
EIEADVNDTS LLLSGDHSIQ QQLQEVREDD DDAEMTHSVA VNVYPATSRM PKLTIVVVDT 180
IPVELKSSYM VWSWFIYVLS ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN 240
PATTRELTSL VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV 300
SDAEPVMLEQ ISRISQQIGY YLHRASMRGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV 360
NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI 420
PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITEQYEGKI VAGESMLGGA RMEVIFGRQH 480
SAPKDE 486 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IMP:EcoCyc. GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc. GO:0010350; P:cellular response to magnesium starvation; IMP:EcoCyc. GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro. GO:0046777; P:protein autophosphorylation; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |