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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1430 [new locus tag: SACOL_RS07285 ]
  • pan locus tag?: SAUPAN003808000
  • symbol: dapA
  • pan gene symbol?: dapA
  • synonym:
  • product: dihydrodipicolinate synthase

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1430 [new locus tag: SACOL_RS07285 ]
  • symbol: dapA
  • product: dihydrodipicolinate synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 1442861..1443748
  • length: 888
  • essential: unknown other strains

Accession numbers[edit | edit source]

Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    ATGACACATTTATTTGAGGGTGTTGGCGTTGCACTTACAACCCCTTTTACAAATAACAAA
    GTTAATATTGAAGCTTTGAAAACACACGTTAATTTTTTACTAGAAAATAATGCCCAAGCA
    ATCATCGTTAATGGAACTACTGCTGAGAGCCCTACTTTAACAACAGATGAAAAAGAACGC
    ATTCTAAAAACAGTTATTGATCTTGTAGATAAACGTGTTCCTGTCATAGCAGGAACTGGC
    ACTAATGATACTGAAAAGTCAATCCAAGCTTCAATCCAAGCTAAAGCCTTAGGGGCTGAT
    GCAATTATGTTAATTACGCCCTACTACAACAAAACGAACCAACGTGGTTTAGTCAAACAC
    TTTGAAGCGATTGCAGATGCTGTGAAATTACCAGTCGTGCTGTACAATGTTCCTTCAAGA
    ACGAACATGACAATTGAACCAGAAACTGTAGAAATATTAAGTCAACATCCTTATATAGTT
    GCTTTAAAAGATGCTACGAATGATTTTGAGTATTTAGAAGAAGTGAAAAAGCGCATTGAT
    ACAAATTCATTTGCATTATATAGTGGCAATGATGACAACGTCGTCGAATACTATCAACGT
    GGCGGTCAAGGGGTTATCTCTGTTATTGCCAATGTCATTCCTAAAGAATTTCAAGCGTTA
    TACGATGCTCAACAAAGTGGATTAGATATTCAAGATCAATTTAAACCAATCGGCACACTG
    TTATCAGCTTTATCAGTTGATATTAACCCAATTCCTATTAAAGCTCTAACAAGTTATTTA
    GGATTTGGAAATTATGAATTACGTCTACCATTGGTTAGCCTAGAAGATACAGATACTAAA
    GTGCTTCGTGAAACATATGACACATTTAAAGCGGGTGAAAATGAGTGA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    888

Protein[edit | edit source]

Protein Data Bank: 3DI0
Protein Data Bank: 3DI1

General[edit | edit source]

  • locus tag: SACOL1430 [new locus tag: SACOL_RS07285 ]
  • symbol: DapA
  • description: dihydrodipicolinate synthase
  • length: 295
  • theoretical pI: 4.5405
  • theoretical MW: 32583.7
  • GRAVY: -0.155254

Function[edit | edit source]

  • reaction:
    EC 4.3.3.7?  ExPASy
    4-hydroxy-tetrahydrodipicolinate synthase Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O
    EC 4.2.1.52?  ExPASy
    Transferred entry: 4.3.3.7
  • TIGRFAM:
    Metabolism Amino acid biosynthesis Aspartate family 4-hydroxy-tetrahydrodipicolinate synthase (TIGR00674; EC 4.3.3.7; HMM-score: 282)
    and 6 more
    2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase (TIGR02313; EC 4.1.2.-; HMM-score: 193.2)
    5-dehydro-4-deoxyglucarate dehydratase (TIGR03249; EC 4.2.1.41; HMM-score: 110.3)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides N-acetylneuraminate lyase (TIGR00683; EC 4.1.3.3; HMM-score: 96.8)
    Metabolism Central intermediary metabolism Amino sugars N-acetylneuraminate lyase (TIGR00683; EC 4.1.3.3; HMM-score: 96.8)
    Hypothetical proteins Conserved TIGR01244 family protein (TIGR01244; HMM-score: 13.8)
    Metabolism Amino acid biosynthesis Serine family putative phosphoserine aminotransferase (TIGR01366; EC 2.6.1.52; HMM-score: 13.2)
  • TheSEED  :
    • 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7)
    Amino Acids and Derivatives Lysine, threonine, methionine, and cysteine Lysine Biosynthesis DAP Pathway  4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7)
  • PFAM:
    TIM_barrel (CL0036) DHDPS; Dihydrodipicolinate synthetase family (PF00701; HMM-score: 250.8)
    and 3 more
    Tubulin_C (CL0442) FtsZ_C; FtsZ family, C-terminal domain (PF12327; HMM-score: 15.3)
    TIM_barrel (CL0036) NMO; Nitronate monooxygenase (PF03060; HMM-score: 13.6)
    SIS (CL0067) SIS; SIS domain (PF01380; HMM-score: 13.3)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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): 0.009594
    • TAT(Tat/SPI): 0.000492
    • LIPO(Sec/SPII): 0.000627
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MTHLFEGVGVALTTPFTNNKVNIEALKTHVNFLLENNAQAIIVNGTTAESPTLTTDEKERILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLRETYDTFKAGENE

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 1303 [4]
  • interaction partners:
    SACOL1385(acnA)aconitate hydratase  [5] (data from MRSA252)
    SACOL2218(adk)adenylate kinase  [5] (data from MRSA252)
    SACOL0154(aldA1)aldehyde dehydrogenase  [5] (data from MRSA252)
    SACOL2656(arcB2)ornithine carbamoyltransferase  [5] (data from MRSA252)
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1215(carB)carbamoyl phosphate synthase large subunit  [5] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [5] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0937(dltC)D-alanine--poly(phosphoribitol) ligase subunit 2  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0634(eutD)phosphotransacetylase  [5] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [5] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [5] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [5] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [5] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [5] (data from MRSA252)
    SACOL2415(gpmA)phosphoglyceromutase  [5] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [5] (data from MRSA252)
    SACOL2017(groES)co-chaperonin GroES  [5] (data from MRSA252)
    SACOL0461(guaA)GMP synthase  [5] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SACOL1368(kataA)catalase  [5] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL1509(ndk)nucleoside diphosphate kinase  [5] (data from MRSA252)
    SACOL1285(nusA)transcription elongation factor NusA  [5] (data from MRSA252)
    SACOL1838(pckA)phosphoenolpyruvate carboxykinase  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [5] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [5] (data from MRSA252)
    SACOL0841(pgm)phosphoglyceromutase  [5] (data from MRSA252)
    SACOL1982(ppaC)manganese-dependent inorganic pyrophosphatase  [5] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [5] (data from MRSA252)
    SACOL1092(ptsI)phosphoenolpyruvate-protein phosphotransferase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL1213(pyrC)dihydroorotase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL2228(rplX)50S ribosomal protein L24  [5] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [5] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL1254(rpsP)30S ribosomal protein S16  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [5] (data from MRSA252)
    SACOL1831(tal)translaldolase  [5] (data from MRSA252)
    SACOL1722(tig)trigger factor  [5] (data from MRSA252)
    SACOL1155(trxA)thioredoxin  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL0426acetyl-CoA acetyltransferase  [5] (data from MRSA252)
    SACOL0457hypothetical protein  [5] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [5] (data from MRSA252)
    SACOL0617hexulose-6-phosphate synthase  [5] (data from MRSA252)
    SACOL0688ABC transporter substrate-binding protein  [5] (data from MRSA252)
    SACOL0727hypothetical protein  [5] (data from MRSA252)
    SACOL0875thioredoxin  [5] (data from MRSA252)
    SACOL0876hypothetical protein  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [5] (data from MRSA252)
    SACOL1020hypothetical protein  [5] (data from MRSA252)
    SACOL1098hypothetical protein  [5] (data from MRSA252)
    SACOL1593glycine dehydrogenase subunit 2  [5] (data from MRSA252)
    SACOL1594glycine dehydrogenase subunit 1  [5] (data from MRSA252)
    SACOL1670hypothetical protein  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL1801dipeptidase PepV  [5] (data from MRSA252)
    SACOL1952ferritins family protein  [5] (data from MRSA252)
    SACOL1992hypothetical protein  [5] (data from MRSA252)
    SACOL2296glycerate dehydrogenase  [5] (data from MRSA252)
    SACOL2553pyruvate oxidase  [5] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [5] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [5] (data from MRSA252)

Expression & Regulation[edit | edit source]

Regulation[edit | edit source]

  • regulators: L-box (transcription termination) regulon, CodY (repression) regulon
    L-box(RNA)important in Lysine biosynthesis; transcription unit transferred from N315 data RegPrecise 
    CodY(TF)important in Amino acid metabolism; RegPrecise    transcription unit transferred from N315 data RegPrecise 

Transcription pattern[edit | edit source]

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

Protein stability[edit | edit source]

  • half-life: 22.68 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. 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)
  2. 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)
  3. 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)
  4. 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)
  5. 5.000 5.001 5.002 5.003 5.004 5.005 5.006 5.007 5.008 5.009 5.010 5.011 5.012 5.013 5.014 5.015 5.016 5.017 5.018 5.019 5.020 5.021 5.022 5.023 5.024 5.025 5.026 5.027 5.028 5.029 5.030 5.031 5.032 5.033 5.034 5.035 5.036 5.037 5.038 5.039 5.040 5.041 5.042 5.043 5.044 5.045 5.046 5.047 5.048 5.049 5.050 5.051 5.052 5.053 5.054 5.055 5.056 5.057 5.058 5.059 5.060 5.061 5.062 5.063 5.064 5.065 5.066 5.067 5.068 5.069 5.070 5.071 5.072 5.073 5.074 5.075 5.076 5.077 5.078 5.079 5.080 5.081 5.082 5.083 5.084 5.085 5.086 5.087 5.088 5.089 5.090 5.091 5.092 5.093 5.094 5.095 5.096 5.097 5.098 5.099 5.100 5.101 5.102 5.103 5.104 5.105 5.106 5.107 5.108 5.109 5.110 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)
  6. 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]

Tavarekere S Girish, Eshita Sharma, B Gopal
Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase.
FEBS Lett: 2008, 582(19);2923-30
[PubMed:18671976] [WorldCat.org] [DOI] (P p)