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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL2313 [new locus tag: SACOL_RS12165 ]
- pan locus tag?: SAUPAN005800000
- symbol: SACOL2313
- pan gene symbol?: —
- synonym:
- product: HAD superfamily hydrolase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL2313 [new locus tag: SACOL_RS12165 ]
- symbol: SACOL2313
- product: HAD superfamily hydrolase
- replicon: chromosome
- strand: -
- coordinates: 2373597..2374232
- length: 636
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238157 NCBI
- RefSeq: YP_187120 NCBI
- BioCyc:
- MicrobesOnline: 913795 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: SACOL2313 [new locus tag: SACOL_RS12165 ]
- symbol: SACOL2313
- description: HAD superfamily hydrolase
- 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 & 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) SACOL0842 (eno) phosphopyruvate hydratase [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL2618 (ldh2) L-lactate dehydrogenase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [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) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [1] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [1] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [1] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [1] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [1] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [1] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [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) SACOL2206 (rpsI) 30S ribosomal protein S9 [1] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [1] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [1] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL2173 alkaline shock protein 23 [1] (data from MRSA252)
⊟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: PeptideAtlasquantitative data / protein copy number per cell: 328 [5]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟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: 39.27 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 1.28 1.29 1.30 1.31
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) - ↑
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]