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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
- pan locus tag?: SAUPAN006297000
- symbol: ldh2
- pan gene symbol?: ldh2
- synonym:
- product: L-lactate dehydrogenase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
- symbol: ldh2
- product: L-lactate dehydrogenase
- replicon: chromosome
- strand: -
- coordinates: 2674414..2675373
- length: 960
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237174 NCBI
- RefSeq: YP_187407 NCBI
- BioCyc:
- MicrobesOnline: 914086 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGAAAACATTTGGTAAAAAGGTTGTATTAATCGGAGATGGATCTGTAGGATCAAGCTAT
GCCTTTGCAATGGTTACGCAAGGTGTTGCTGATGAATTTGTAATTATTGACATTGCAAAA
GACAAAGTAAAAGCAGATGTTCAAGATTTAAACCATGGTACAGTCCACAGTCCTTCACCA
GTTGATGTGAAAGCAGGTGAATACGAAGACTGTAAAGATGCAGATTTAGTTGTTATTACA
GCTGGCGCACCTCAAAAGCCAGGTGAAACACGTTTACAATTAGTTGAAAAAAATACTAAG
ATTATGAAGAGCATCGTTAAGAGTGTTATGGATAGTGGCTTTGATGGATATTTCTTAATC
GCGGCAAACCCTGTAGACATTTTAACAAGATTTGTAAAAGAATATACTGGATTACCAGCA
GAGCGTGTTATCGGTTCAGGTACTGTATTGGACAGTGCACGTTTACAATATTTAATTAGC
CAAGAACTTGGTGTTGCACCTTCAAGTGTTGACGCTAGTATTATTGGCGAGCATGGTGAT
ACTGAACTTGCAGTTTGGTCACAAGCAAATGTAGCAGGTATTTCAGTATATGACACATTA
AAAGAACAAACTGGTAGCGAAGCTAAAGCGGAAGAAATTTATGTGAATACACGTGACGCT
GCTTATGAAATTATCCAAGCTAAAGGGTCAACATACTATGGTATTGCATTAGCATTGATG
CGCATTTCAAAAGCCATTTTAAATAATGAAAATAATGTCTTAAATGTTTCTATACAATTA
GATGGTCAATATGGTGGTCACAAAGGCGTTTACCTAGGTGTACCAACATTAGTTAACCAA
CATGGCGCAGTTAAAATTTATGAAATGCCATTAAGTGCCGAAGAACAAGCGTTGTTCGAT
AAATCTGTTAAAACATTAGAAGATACATTTGATTCAATTAAATATTTATTAGAAGACTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
- symbol: Ldh2
- description: L-lactate dehydrogenase
- length: 319
- theoretical pI: 4.53599
- theoretical MW: 34419.8
- GRAVY: -0.0498433
⊟Function[edit | edit source]
- reaction: EC 1.1.1.27? ExPASyL-lactate dehydrogenase (S)-lactate + NAD+ = pyruvate + NADH
- TIGRFAM: Energy metabolism Anaerobic L-lactate dehydrogenase (TIGR01771; EC 1.1.1.27; HMM-score: 420.6)Energy metabolism Glycolysis/gluconeogenesis L-lactate dehydrogenase (TIGR01771; EC 1.1.1.27; HMM-score: 420.6)and 9 moreEnergy metabolism TCA cycle malate dehydrogenase, NAD-dependent (TIGR01763; EC 1.1.1.37; HMM-score: 209.2)Energy metabolism TCA cycle malate dehydrogenase, NAD-dependent (TIGR01772; EC 1.1.1.37; HMM-score: 72.2)malate dehydrogenase (TIGR01759; EC 1.1.1.-; HMM-score: 68.5)lactate dehydrogenase (TIGR01756; EC 1.1.1.27; HMM-score: 51)malate dehydrogenase, NAD-dependent (TIGR01758; EC 1.1.1.37; HMM-score: 47.1)malate dehydrogenase, NADP-dependent (TIGR01757; EC 1.1.1.82; HMM-score: 17.8)Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylD (TIGR03911; HMM-score: 15.7)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiazole biosynthesis adenylyltransferase ThiF (TIGR02356; EC 2.7.7.73; HMM-score: 12.4)nucleotide sugar dehydrogenase (TIGR03026; HMM-score: 12.2)
- TheSEED: and 1 more
- PFAM: NADP_Rossmann (CL0063) Ldh_1_N; lactate/malate dehydrogenase, NAD binding domain (PF00056; HMM-score: 153.1)and 5 moreLDH_C (CL0341) Ldh_1_C; lactate/malate dehydrogenase, alpha/beta C-terminal domain (PF02866; HMM-score: 122.2)NADP_Rossmann (CL0063) Sacchrp_dh_NADP; Saccharopine dehydrogenase NADP binding domain (PF03435; HMM-score: 16.6)NAD_binding_7; Putative NAD(P)-binding (PF13241; HMM-score: 15.4)UDPG_MGDP_dh_N; UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain (PF03721; HMM-score: 15.2)F420_oxidored; NADP oxidoreductase coenzyme F420-dependent (PF03807; HMM-score: 14.9)
⊟Structure, modifications & interactions[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
- protein partners:
SACOL1637 (dnaK) molecular chaperone DnaK [1] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL1477 (ilvA1) threonine dehydratase [1] (data from MRSA252) SACOL0173 (ipdC) indole-3-pyruvate decarboxylase [1] (data from MRSA252) SACOL0033 (mecA) penicillin-binding protein 2' [1] (data from MRSA252) SACOL2272 (modA) molybdenum ABC transporter molybdenum-binding protein ModA [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) SACOL1745 (pyk) pyruvate kinase [1] (data from MRSA252) SACOL1277 (pyrH) uridylate kinase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [1] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [1] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [1] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [1] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [1] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [1] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [1] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [1] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [1] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [1] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [1] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [1] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [1] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [1] (data from MRSA252) SACOL0439 (rpsR) 30S ribosomal protein S18 [1] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [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) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL0599 hypothetical protein [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) SACOL2173 alkaline shock protein 23 [1] (data from MRSA252)
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- 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): 0.108195
- TAT(Tat/SPI): 0.002687
- LIPO(Sec/SPII): 0.004804
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKTFGKKVVLIGDGSVGSSYAFAMVTQGVADEFVIIDIAKDKVKADVQDLNHGTVHSPSPVDVKAGEYEDCKDADLVVITAGAPQKPGETRLQLVEKNTKIMKSIVKSVMDSGFDGYFLIAANPVDILTRFVKEYTGLPAERVIGSGTVLDSARLQYLISQELGVAPSSVDASIIGEHGDTELAVWSQANVAGISVYDTLKEQTGSEAKAEEIYVNTRDAAYEIIQAKGSTYYGIALALMRISKAILNNENNVLNVSIQLDGQYGGHKGVYLGVPTLVNQHGAVKIYEMPLSAEEQALFDKSVKTLEDTFDSIKYLLED
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlasquantitative data / protein copy number per cell: 812 [6]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- ldh2 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: 38.03 h [7]
⊟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 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 1.43 1.44 1.45 1.46 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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ 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]
Anthony R Richardson, Stephen J Libby, Ferric C Fang
A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity.
Science: 2008, 319(5870);1672-6
[PubMed:18356528] [WorldCat.org] [DOI] (I p)