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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02703
- pan locus tag?: SAUPAN005952000
- symbol: gpmA
- pan gene symbol?: gpmA
- synonym:
- product: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_02703
- symbol: gpmA
- product: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- replicon: chromosome
- strand: -
- coordinates: 2484752..2485438
- length: 687
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3919722 NCBI
- RefSeq: YP_501165 NCBI
- BioCyc: G1I0R-2549 BioCyc
- MicrobesOnline: 1291136 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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661ATGCCAAAATTAATTTTATGTCGTCATGGACAAAGCGAGTGGAATGCTAAAAACTTATTT
ACTGGATGGGAAGATGTTAATTTATCTGAACAAGGTATTAATGAAGCGACTAGAGCAGGT
GAAAAAGTAAGAGAAAATAACATTGCCATCGATGTAGCTTTTACATCGTTATTAACACGT
GCTTTAGATACAACGCATTATATTTTAACTGAATCTAAACAACAATGGATTCCTGTATAT
AAAAGCTGGCGTTTAAATGAACGCCACTATGGTGGATTGCAAGGCTTAAATAAAGATGAT
GCTAGAAAAGAATTTGGAGAAGAACAAGTACATATTTGGCGTCGTTCTTATGATGTGAAA
CCACCTGCTGAAACCGAAGAACAACGTGAAGCTTACTTAGCTGATCGTCGATATAATCAT
TTAGATAAACGTATGATGCCTTATTCTGAAAGTCTGAAAGATACTTTAGTTCGAGTGATA
CCATTTTGGACAGATCATATTTCACAATATTTGCTAGATGGTCAAACGGTATTAGTTTCT
GCACACGGAAATTCAATTCGCGCATTGATTAAATATCTTGAAGATGTGTCAGATGAAGAT
ATCATTAATTATGAAATTAAAACAGGTGCACCGCTTGTTTATGAATTAACGGATGATTTA
GAAGTTATAGATAAATACTACTTATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02703
- symbol: GpmA
- description: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- length: 228
- theoretical pI: 5.05486
- theoretical MW: 26679.8
- GRAVY: -0.632018
⊟Function[edit | edit source]
- reaction: EC 5.4.2.1? ExPASyTransferred entry: 5.4.2.11 and 5.4.2.12EC 5.4.2.11? ExPASyPhosphoglycerate mutase (2,3-diphosphoglycerate-dependent) 2-phospho-D-glycerate = 3-phospho-D-glycerate
- TIGRFAM: phosphoglycerate mutase 1 family (TIGR01258; HMM-score: 332.9)and 3 moreBiosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin alpha-ribazole phosphatase (TIGR03162; EC 3.1.3.73; HMM-score: 79.1)probable phosphomutase, MSMEG_4193 family (TIGR03848; EC 5.4.2.-; HMM-score: 39.2)Regulatory functions Protein interactions phosphohistidine phosphatase SixA (TIGR00249; EC 3.1.3.-; HMM-score: 22.7)
- TheSEED :
- Phosphoglycerate mutase (EC 5.4.2.11)
Carbohydrates Central carbohydrate metabolism Glycolysis and Gluconeogenesis Phosphoglycerate mutase (EC 5.4.2.1)and 1 more - PFAM: His_phosphatase (CL0071) His_Phos_1; Histidine phosphatase superfamily (branch 1) (PF00300; HMM-score: 127.6)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: unknown (no significant prediction)
- Cytoplasmic Score: 2.5
- Cytoplasmic Membrane Score: 2.5
- Cellwall Score: 2.5
- Extracellular Score: 2.5
- 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): 0.006454
- TAT(Tat/SPI): 0.000508
- LIPO(Sec/SPII): 0.001283
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVYKSWRLNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETEEQREAYLADRRYNHLDKRMMPYSESLKDTLVRVIPFWTDHISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDIINYEIKTGAPLVYELTDDLEVIDKYYL
⊟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_00943 (ppnK) inorganic polyphosphate/ATP-NAD kinase [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02505 (rplP) 50S ribosomal protein L16 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [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_00348 (rpsF) 30S ribosomal protein S6 [3] (data from MRSA252) SAOUHSC_00527 (rpsL) 30S ribosomal protein S12 [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_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [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_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [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 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 4.2 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)