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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL2415 [new locus tag: SACOL_RS12675 ]
- pan locus tag?: SAUPAN005952000
- symbol: gpmA
- pan gene symbol?: gpmA
- synonym:
- product: phosphoglyceromutase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL2415 [new locus tag: SACOL_RS12675 ]
- symbol: gpmA
- product: phosphoglyceromutase
- replicon: chromosome
- strand: -
- coordinates: 2474088..2474774
- length: 687
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238336 NCBI
- RefSeq: YP_187218 NCBI
- BioCyc:
- MicrobesOnline: 913895 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: SACOL2415 [new locus tag: SACOL_RS12675 ]
- symbol: GpmA
- description: phosphoglyceromutase
- 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: Carbohydrates Central carbohydrate metabolism Glycolysis and Gluconeogenesis Phosphoglycerate mutase (EC 5.4.2.1)and 2 morePhosphoglycerate mutase (EC 5.4.2.11)
- PFAM: His_phosphatase (CL0071) His_Phos_1; Histidine phosphatase superfamily (branch 1) (PF00300; HMM-score: 127.6)
⊟Structure, modifications & interactions[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
- protein partners:
SACOL2657 (arcA) arginine deiminase [1] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [1] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [1] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [1] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [1] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [1] (data from MRSA252) SACOL1011 (ppnK) inorganic polyphosphate/ATP-NAD kinase [1] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [1] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [1] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [1] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [1] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [1] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [1] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [1] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [1] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [1] (data from MRSA252) SACOL0944 NADH dehydrogenase [1] (data from MRSA252) SACOL1759 universal stress protein [1] (data from MRSA252)
⊟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: PeptideAtlasquantitative data / protein copy number per cell: 1292 [5]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- gpmA no polycistronic organisation predicted
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 23.1 h [6]
⊟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]
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27
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) - ↑
Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑
Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑
Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑
Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑
Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)
⊟Relevant publications[edit | edit source]