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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]
- Gene ID: 3236210 NCBI
- RefSeq: YP_186282 NCBI
- BioCyc: see SACOL_RS07285
- MicrobesOnline: 912888 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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841ATGACACATTTATTTGAGGGTGTTGGCGTTGCACTTACAACCCCTTTTACAAATAACAAA
GTTAATATTGAAGCTTTGAAAACACACGTTAATTTTTTACTAGAAAATAATGCCCAAGCA
ATCATCGTTAATGGAACTACTGCTGAGAGCCCTACTTTAACAACAGATGAAAAAGAACGC
ATTCTAAAAACAGTTATTGATCTTGTAGATAAACGTGTTCCTGTCATAGCAGGAACTGGC
ACTAATGATACTGAAAAGTCAATCCAAGCTTCAATCCAAGCTAAAGCCTTAGGGGCTGAT
GCAATTATGTTAATTACGCCCTACTACAACAAAACGAACCAACGTGGTTTAGTCAAACAC
TTTGAAGCGATTGCAGATGCTGTGAAATTACCAGTCGTGCTGTACAATGTTCCTTCAAGA
ACGAACATGACAATTGAACCAGAAACTGTAGAAATATTAAGTCAACATCCTTATATAGTT
GCTTTAAAAGATGCTACGAATGATTTTGAGTATTTAGAAGAAGTGAAAAAGCGCATTGAT
ACAAATTCATTTGCATTATATAGTGGCAATGATGACAACGTCGTCGAATACTATCAACGT
GGCGGTCAAGGGGTTATCTCTGTTATTGCCAATGTCATTCCTAAAGAATTTCAAGCGTTA
TACGATGCTCAACAAAGTGGATTAGATATTCAAGATCAATTTAAACCAATCGGCACACTG
TTATCAGCTTTATCAGTTGATATTAACCCAATTCCTATTAAAGCTCTAACAAGTTATTTA
GGATTTGGAAATTATGAATTACGTCTACCATTGGTTAGCCTAGAAGATACAGATACTAAA
GTGCTTCGTGAAACATATGACACATTTAAAGCGGGTGAAAATGAGTGA60
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⊟Protein[edit | edit source]
⊟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? ExPASy4-hydroxy-tetrahydrodipicolinate synthase Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2OEC 4.2.1.52? ExPASyTransferred entry: 4.3.3.7
- TIGRFAM: Amino acid biosynthesis Aspartate family 4-hydroxy-tetrahydrodipicolinate synthase (TIGR00674; EC 4.3.3.7; HMM-score: 282)and 6 more2,4-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 envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides N-acetylneuraminate lyase (TIGR00683; EC 4.1.3.3; HMM-score: 96.8)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)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)
- PFAM: TIM_barrel (CL0036) DHDPS; Dihydrodipicolinate synthetase family (PF00701; HMM-score: 250.8)and 3 moreTubulin_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) SACOL0426 acetyl-CoA acetyltransferase [5] (data from MRSA252) SACOL0457 hypothetical protein [5] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [5] (data from MRSA252) SACOL0617 hexulose-6-phosphate synthase [5] (data from MRSA252) SACOL0688 ABC transporter substrate-binding protein [5] (data from MRSA252) SACOL0727 hypothetical protein [5] (data from MRSA252) SACOL0875 thioredoxin [5] (data from MRSA252) SACOL0876 hypothetical protein [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [5] (data from MRSA252) SACOL1020 hypothetical protein [5] (data from MRSA252) SACOL1098 hypothetical protein [5] (data from MRSA252) SACOL1593 glycine dehydrogenase subunit 2 [5] (data from MRSA252) SACOL1594 glycine dehydrogenase subunit 1 [5] (data from MRSA252) SACOL1670 hypothetical protein [5] (data from MRSA252) SACOL1753 universal stress protein [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252) SACOL1801 dipeptidase PepV [5] (data from MRSA252) SACOL1952 ferritins family protein [5] (data from MRSA252) SACOL1992 hypothetical protein [5] (data from MRSA252) SACOL2296 glycerate dehydrogenase [5] (data from MRSA252) SACOL2553 pyruvate oxidase [5] (data from MRSA252) SACOL2561 hydroxymethylglutaryl-CoA synthase [5] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[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]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟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]
- ↑ 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) - ↑ 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) - ↑ 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)