NCBI: 26-AUG-2013

⊟Summary[edit | edit source]

organism: Staphylococcus aureus N315

locus tag: SA2204 [new locus tag: SA_RS12645 ]

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: SA2204 [new locus tag: SA_RS12645 ]
symbol: gpmA
product: phosphoglyceromutase
replicon: chromosome
strand: -
coordinates: 2473572..2474258
length: 687
essential: no DEG other strains

⊟Accession numbers[edit | edit source]

Gene ID: 1125132 NCBI
RefSeq: NP_375527 NCBI
BioCyc: see SA_RS12645
MicrobesOnline: 104553 MicrobesOnline

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

1
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481
541
601
661
ATGCCAAAATTAATTTTATGTCGTCATGGACAAAGCGAGTGGAATGCTAAAAACTTATTT
ACTGGATGGGAAGATGTTAATTTATCTGAACAAGGTATTAATGAAGCGACTAGAGCAGGT
GAAAAAGTAAGAGAAAATAACATTGCCATCGATGTAGCTTTTACATCGTTATTAACACGT
GCTTTAGATACAACGCATTATATTTTAACTGAATCTAAACAACAATGGATTCCTGTATAT
AAAAGCTGGCGTTTAAATGAACGCCACTATGGTGGATTGCAAGGCTTAAATAAAGATGAT
GCTAGAAAAGAATTTGGAGAAGAACAAGTACATATTTGGCGTCGTTCTTATGATGTGAAA
CCACCTGCTGAAACCGAAGAACAACGTGAAGCTTACTTAGCTGATCGTCGATATAATCAT
TTAGATAAACGTATGATGCCTTATTCTGAAAGTCTGAAAGATACTTTAGTTCGAGTGATA
CCATTTTGGACAGATCATATTTCACAATATTTGCTAGATGGTCAAACGGTATTAGTTTCT
GCACACGGAAATTCAATTCGCGCATTAATTAAATATCTTGAAGATGTGTCAGATGAAGAT
ATCATTAATTATGAAATTAAAACAGGTGCACCGCTTGTTTATGAATTAACGGATGATTTA
GAAGTTATAGATAAATACTACTTATAA
60
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300
360
420
480
540
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660
687

⊟Protein[edit | edit source]

⊟General[edit | edit source]

locus tag: SA2204 [new locus tag: SA_RS12645 ]
symbol: GpmA
description: phosphoglyceromutase
length: 228
theoretical pI: 5.05486
theoretical MW: 26679.8
GRAVY: -0.632018

⊟Function[edit | edit source]

⊞⊞reaction:
EC 5.4.2.11? ExPASy
Phosphoglycerate 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 more
Metabolism Biosynthesis 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)
Signal transduction 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
Carbohydrates Central carbohydrate metabolism Glycolysis and Gluconeogenesis Phosphoglycerate mutase (EC 5.4.2.11)
PFAM:
His_phosphatase (CL0071) His_Phos_1; Histidine phosphatase superfamily (branch 1) (PF00300; HMM-score: 125.4)

⊟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
⊞⊞
DeepLocPro: Cytoplasmic
- Cytoplasmic Score: 0.9951
- Cytoplasmic Membrane Score: 0.0014
- Cell wall & surface Score: 0.0001
- Extracellular Score: 0.0034
⊞⊞
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]

GI: 15927994 NCBI
RefSeq: NP_375527 NCBI
UniProt: P99153 UniProt

⊟Protein sequence[edit | edit source]

MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVYKSWRLNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETEEQREAYLADRRYNHLDKRMMPYSESLKDTLVRVIPFWTDHISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDIINYEIKTGAPLVYELTDDLEVIDKYYL

⊟Experimental data[edit | edit source]

experimentally validated: data available for COL, NCTC8325
protein localization: data available for COL
quantitative data / protein copy number per cell: data available for COL

⊟⊟interaction partners:

SA2428	(arcA)	arginine deiminase ^[1] (data from MRSA252)
SA1517	(citC)	isocitrate dehydrogenase ^[1] (data from MRSA252)
SA1409	(dnaK)	molecular chaperone DnaK ^[1] (data from MRSA252)
SA0505	(fus)	elongation factor G ^[1] (data from MRSA252)
SA1305	(hu)	DNA-binding protein II ^[1] (data from MRSA252)
SA1244	(odhB)	dihydrolipoamide succinyltransferase ^[1] (data from MRSA252)
SA0943-1	(pdhA)	pyruvate dehydrogenase E1 component subunit alpha ^[1] (data from MRSA252)
SA0944	(pdhB)	pyruvate dehydrogenase E1 component subunit beta ^[1] (data from MRSA252)
SA0945	(pdhC)	branched-chain alpha-keto acid dehydrogenase E2 subunit ^[1] (data from MRSA252)
SA0946	(pdhD)	dihydrolipoamide dehydrogenase ^[1] (data from MRSA252)
SA0218	(pflB)	formate acetyltransferase ^[1] (data from MRSA252)
SA0865	(ppnK)	inorganic polyphosphate/ATP-NAD kinase ^[1] (data from MRSA252)
SA1520	(pykA)	pyruvate kinase ^[1] (data from MRSA252)
SA0497	(rplJ)	50S ribosomal protein L10 ^[1] (data from MRSA252)
SA2029	(rplO)	50S ribosomal protein L15 ^[1] (data from MRSA252)
SA2040	(rplP)	50S ribosomal protein L16 ^[1] (data from MRSA252)
SA1084	(rplS)	50S ribosomal protein L19 ^[1] (data from MRSA252)
SA1473	(rplU)	50S ribosomal protein L21 ^[1] (data from MRSA252)
SA1099	(rpsB)	30S ribosomal protein S2 ^[1] (data from MRSA252)
SA2041	(rpsC)	30S ribosomal protein S3 ^[1] (data from MRSA252)
SA2031	(rpsE)	30S ribosomal protein S5 ^[1] (data from MRSA252)
SA0352	(rpsF)	30S ribosomal protein S6 ^[1] (data from MRSA252)
SA0503	(rpsL)	30S ribosomal protein S12 ^[1] (data from MRSA252)
SA0107	(spa)	immunoglobulin G binding protein A ^[1] (data from MRSA252)
SA0506	(tuf)	elongation factor Tu ^[1] (data from MRSA252)
SA0627		hypothetical protein ^[1] (data from MRSA252)
SA0802		hypothetical protein ^[1] (data from MRSA252)
SA1532		hypothetical protein ^[1] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

MicrobesOnline: 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]

Aureolib: data available for COL

⊟Protein stability[edit | edit source]

half-life: no data available

⊞Biological Material[edit | edit source]

⊞Other Information[edit | edit source]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

↑ ^{Jump up to: 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)

⊟Relevant publications[edit | edit source]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J Microbiol Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)

[pubmed21166474-1] {Jump up to: 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)

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⊟Summary[edit | edit source]

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟DNA sequence[edit | edit source]

⊟Protein[edit | edit source]

⊟General[edit | edit source]

⊟Function[edit | edit source]

⊟Structure, modifications & cofactors[edit | edit source]

⊟Localization[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

⊟Experimental data[edit | edit source]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

⊞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]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]

⊟Summary[edit | edit source]

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟DNA sequence[edit | edit source]

⊟Protein[edit | edit source]

⊟General[edit | edit source]

⊟Function[edit | edit source]

⊟Structure, modifications & cofactors[edit | edit source]

⊟Localization[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

⊟Experimental data[edit | edit source]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

⊞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]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]