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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02594
- pan locus tag?: SAUPAN005800000
- symbol: SAOUHSC_02594
- pan gene symbol?: —
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_02594
- symbol: SAOUHSC_02594
- product: hypothetical protein
- replicon: chromosome
- strand: -
- coordinates: 2384263..2384898
- length: 636
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921590 NCBI
- RefSeq: YP_501056 NCBI
- BioCyc: G1I0R-2449 BioCyc
- MicrobesOnline: 1291027 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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601ATGTATAGAGCAGTTATATTTGATTTCGATGGAACAATAATAGATACGGAACAACATTTA
TTTAATGTTATTAATAAACATTTAGAGATGCATAATGCCGATCCTATAAGCATTGATTTT
TATCGTTCTTCTATTGGAGGAGCAGCTACAGATTTGCATGACCATTTAATTAAAGCGATT
GGTTCGGAAAATAAAGATAAACTTTATGAAGAACATCATCTTACTAGTACAACATTACCG
ATGATTGATACGATTAAATCATTGATGGCATTTTTAAAGCAACGTCACATTCCTATGGCA
ATTGCCACAAGTAGTGTGAAAGCGGAAATAATGCCCACCTTTAAAGCATTAGGTCTAGAC
GATTATATAGAGGTAGTTGTTGGTAGAGAAGATGTTGAACAAGTTAAACCTGACCCTGAA
TTATATTTATCTGCAGTACAACAATTAAATTATATGCCGACACAATGTTTGGCTATTGAA
GATTCTGTAAATGGTGCAACAGCCGCGATTGCAGCTGGATTAGATGTTATTGTTAATACG
AATAAAATGACAAGCGCACAGGACTTTTCTAATGTAGATTATGTAGCAAAAGATATTGAT
TACGATCAAATTGTAGCGCGTTTCTTTACGAAATAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02594
- symbol: SAOUHSC_02594
- description: hypothetical protein
- length: 211
- theoretical pI: 4.59654
- theoretical MW: 23569.7
- GRAVY: -0.0682464
⊟Function[edit | edit source]
- TIGRFAM: beta-phosphoglucomutase family hydrolase (TIGR02009; HMM-score: 97.7)Energy metabolism Biosynthesis and degradation of polysaccharides beta-phosphoglucomutase (TIGR01990; EC 5.4.2.6; HMM-score: 83.5)and 21 moreEnergy metabolism Sugars phosphoglycolate phosphatase, bacterial (TIGR01449; EC 3.1.3.18; HMM-score: 75.6)Unknown function Enzymes of unknown specificity HAD hydrolase, family IA, variant 3 (TIGR01509; HMM-score: 64.3)HAD hydrolase, TIGR02253 family (TIGR02253; HMM-score: 57.4)AHBA synthesis associated protein (TIGR01454; HMM-score: 49.3)noncanonical pyrimidine nucleotidase, YjjG family (TIGR02254; EC 3.1.3.5; HMM-score: 40.5)pyrimidine 5'-nucleotidase (TIGR01993; EC 3.1.3.5; HMM-score: 37.9)haloacid dehalogenase, type II (TIGR01428; EC 3.8.1.2; HMM-score: 35.7)HAD hydrolase, REG-2-like, family IA (TIGR02252; HMM-score: 33.2)Unknown function Enzymes of unknown specificity HAD hydrolase, family IA, variant 1 (TIGR01549; HMM-score: 32)Central intermediary metabolism Other 2,3-diketo-5-methylthio-1-phosphopentane phosphatase (TIGR01489; HMM-score: 29.6)Central intermediary metabolism Other phosphonoacetaldehyde hydrolase (TIGR01422; EC 3.11.1.1; HMM-score: 28.1)phosphonatase-like hydrolase (TIGR03351; HMM-score: 26.9)Unknown function Enzymes of unknown specificity HAD phosphoserine phosphatase-like hydrolase, family IB (TIGR01488; HMM-score: 25.2)epoxide hydrolase N-terminal domain-like phosphatase (TIGR02247; HMM-score: 24.5)Unknown function Enzymes of unknown specificity HAD hydrolase, family IIIA (TIGR01662; HMM-score: 24.3)HAD hydrolase, TIGR01548 family (TIGR01548; HMM-score: 22.7)Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides D,D-heptose 1,7-bisphosphate phosphatase (TIGR00213; HMM-score: 19.5)histidinol-phosphate phosphatase domain (TIGR01656; HMM-score: 17.3)HAD phosphatase, family IIIC (TIGR01681; HMM-score: 15.2)Unknown function Enzymes of unknown specificity HAD hydrolase, family IB (TIGR01490; HMM-score: 13.5)phosphoserine phosphatase-like hydrolase, archaeal (TIGR01491; HMM-score: 12.4)
- TheSEED :
- Phosphoglycolate phosphatase
- PFAM: HAD (CL0137) HAD_2; haloacid dehalogenase-like hydrolase (PF13419; HMM-score: 120.9)and 4 moreHydrolase; haloacid dehalogenase-like hydrolase (PF00702; HMM-score: 74.4)HAD; haloacid dehalogenase-like hydrolase (PF12710; HMM-score: 21.1)Hydrolase_like; HAD-hyrolase-like (PF13242; HMM-score: 20.7)Put_Phosphatase; Putative Phosphatase (PF06888; HMM-score: 14.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 7.5
- Cytoplasmic Membrane Score: 1.15
- Cellwall Score: 0.62
- Extracellular Score: 0.73
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.002671
- TAT(Tat/SPI): 0.000207
- LIPO(Sec/SPII): 0.000164
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MYRAVIFDFDGTIIDTEQHLFNVINKHLEMHNADPISIDFYRSSIGGAATDLHDHLIKAIGSENKDKLYEEHHLTSTTLPMIDTIKSLMAFLKQRHIPMAIATSSVKAEIMPTFKALGLDDYIEVVVGREDVEQVKPDPELYLSAVQQLNYMPTQCLAIEDSVNGATAAIAAGLDVIVNTNKMTSAQDFSNVDYVAKDIDYDQIVARFFTK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02505 (rplP) 50S ribosomal protein L16 [3] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p) - ↑ 4.0 4.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)