Jump to navigation
Jump to search
NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1715 [new locus tag: SACOL_RS08760 ]
- pan locus tag?: SAUPAN004283000
- symbol: hemB
- pan gene symbol?: hemB
- synonym:
- product: delta-aminolevulinic acid dehydratase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1715 [new locus tag: SACOL_RS08760 ]
- symbol: hemB
- product: delta-aminolevulinic acid dehydratase
- replicon: chromosome
- strand: -
- coordinates: 1746055..1747029
- length: 975
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238571 NCBI
- RefSeq: YP_186553 NCBI
- BioCyc: see SACOL_RS08760
- MicrobesOnline: 913162 MicrobesOnline
⊟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
901
961ATGAAATTTGATAGACATAGAAGATTGAGATCATCAGCGACAATGAGAGATATGGTTAGA
GAGAATCATGTAAGAAAAGAAGATTTAATATATCCAATTTTTGTAGTTGAAAAAGACGAT
GTGAAAAAAGAAATTAAGTCATTGCCAGGTGTATACCAAATCAGTTTGAATTTACTTGAA
AGTGAATTAAAAGAAGCTTATGACTTAGGCATACGTGCCATTATGTTTTTCGGTGTTCCA
AACTCAAAAGATGATATAGGTACTGGTGCATACATTCACGATGGTGTTATTCAACAGGCA
ACACGTATTGCTAAAAAAATGTATGATGACTTATTAATTGTTGCAGACACTTGTTTATGT
GAATATACTGATCATGGTCATTGTGGCGTGATTGATGACCATACACATGACGTTGACAAT
GATAAATCATTGCCACTACTTGTTAAAACAGCAATTTCTCAAGTGGAAGCTGGTGCTGAT
ATTATTGCGCCAAGTAATATGATGGATGGTTTTGTTGCTGAAATTCGTCGTGGATTAGAT
GAAGCCGGCTATTACAATATTCCTATAATGAGTTATGGTGTCAAGTATGCATCAAGTTTC
TTTGGACCTTTTAGAGATGCAGCAGATTCAGCGCCATCATTTGGGGATAGAAAAACGTAT
CAGATGGACCCTGCTAACCGTTTGGAAGCACTTCGTGAATTAGAAAGTGATCTTAAAGAA
GGGTGCGACATGATGATTGTTAAACCTGCTCTAAGTTATTTAGATATAGTTCGAGATGTT
AAAAATCATACGAATGTTCCAGTTGTTGCATATAATGTGAGTGGAGAATATAGTATGACT
AAAGCAGCGGCACAAAATGGTTGGATAGATGAAGAACGTGTCGTTATGGAACAAATGGTT
TCAATGAAACGTGCAGGTGCTGATATGATTATTACGTATTTTGCAAAGGACATTTGTCGC
TATTTAGATAAATAA60
120
180
240
300
360
420
480
540
600
660
720
780
840
900
960
975
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1715 [new locus tag: SACOL_RS08760 ]
- symbol: HemB
- description: delta-aminolevulinic acid dehydratase
- length: 324
- theoretical pI: 5.03483
- theoretical MW: 36582.6
- GRAVY: -0.283025
⊟Function[edit | edit source]
- reaction: EC 4.2.1.24? ExPASyPorphobilinogen synthase 2 5-aminolevulinate = porphobilinogen + 2 H2O
- TIGRFAM:
- TheSEED :
- Porphobilinogen synthase (EC 4.2.1.24)
- PFAM: TIM_barrel (CL0036) ALAD; Delta-aminolevulinic acid dehydratase (PF00490; HMM-score: 484.7)and 1 moreno clan defined HMA; Heavy-metal-associated domain (PF00403; HMM-score: 14.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Zn2+
- effectors:
⊟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): 0.001992
- TAT(Tat/SPI): 0.000419
- LIPO(Sec/SPII): 0.00056
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKFDRHRRLRSSATMRDMVRENHVRKEDLIYPIFVVEKDDVKKEIKSLPGVYQISLNLLESELKEAYDLGIRAIMFFGVPNSKDDIGTGAYIHDGVIQQATRIAKKMYDDLLIVADTCLCEYTDHGHCGVIDDHTHDVDNDKSLPLLVKTAISQVEAGADIIAPSNMMDGFVAEIRRGLDEAGYYNIPIMSYGVKYASSFFGPFRDAADSAPSFGDRKTYQMDPANRLEALRELESDLKEGCDMMIVKPALSYLDIVRDVKNHTNVPVVAYNVSGEYSMTKAAAQNGWIDEERVVMEQMVSMKRAGADMIITYFAKDICRYLDK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 1316 [4]
- interaction partners:
SACOL1760 (ackA) acetate kinase [5] (data from MRSA252) SACOL2218 (adk) adenylate kinase [5] (data from MRSA252) SACOL0452 (ahpC) alkyl hydroperoxide reductase subunit C [5] (data from MRSA252) SACOL0154 (aldA1) aldehyde dehydrogenase [5] (data from MRSA252) SACOL1272 (codY) transcriptional repressor CodY [5] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [5] (data from MRSA252) SACOL2130 (deoD) purine nucleoside phosphorylase [5] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [5] (data from MRSA252) SACOL0002 (dnaN) DNA polymerase III subunit beta [5] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [5] (data from MRSA252) SACOL0634 (eutD) phosphotransacetylase [5] (data from MRSA252) SACOL1245 (fabG1) 3-oxoacyl-ACP reductase [5] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [5] (data from MRSA252) SACOL2117 (fbaA) fructose-bisphosphate aldolase [5] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [5] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [5] (data from MRSA252) SACOL1072 (folD) bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [5] (data from MRSA252) SACOL1278 (frr) ribosome recycling factor [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) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [5] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [5] (data from MRSA252) SACOL0877 (gcvH) glycine cleavage system protein H [5] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [5] (data from MRSA252) SACOL1742 (gltA) citrate synthase [5] (data from MRSA252) SACOL1554 (gnd) 6-phosphogluconate dehydrogenase [5] (data from MRSA252) SACOL1206 (ileS) isoleucyl-tRNA synthetase [5] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [5] (data from MRSA252) SACOL1368 (kataA) catalase [5] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [5] (data from MRSA252) SACOL0562 (lysS) lysyl-tRNA synthetase [5] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [5] (data from MRSA252) SACOL1509 (ndk) nucleoside diphosphate kinase [5] (data from MRSA252) SACOL0582 (nusG) transcription antitermination protein [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) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL1746 (pfkA) 6-phosphofructokinase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [5] (data from MRSA252) SACOL0841 (pgm) phosphoglyceromutase [5] (data from MRSA252) SACOL1982 (ppaC) manganese-dependent inorganic pyrophosphatase [5] (data from MRSA252) SACOL1092 (ptsI) phosphoenolpyruvate-protein phosphotransferase [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [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) SACOL0015 (rplI) 50S ribosomal protein L9 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [5] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [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) 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) SACOL1700 (rpmA) 50S ribosomal protein L27 [5] (data from MRSA252) SACOL2221 (rpmD) 50S ribosomal protein L30 [5] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [5] (data from MRSA252) SACOL1516 (rpsA) 30S ribosomal protein S1 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [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) SACOL2225 (rpsH) 30S ribosomal protein S8 [5] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [5] (data from MRSA252) SACOL2056 (rsbV) anti-anti-sigma factor RsbV [5] (data from MRSA252) SACOL1610 (sodA2) superoxide dismutase [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) SACOL1377 (tkt) transketolase [5] (data from MRSA252) SACOL1762 (tpx) thiol peroxidase [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) SACOL2104 (upp) uracil phosphoribosyltransferase [5] (data from MRSA252) SACOL0179 RpiR family phosphosugar-binding transcriptional regulator [5] (data from MRSA252) SACOL0426 acetyl-CoA acetyltransferase [5] (data from MRSA252) SACOL0521 hypothetical protein [5] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [5] (data from MRSA252) SACOL0596 2-amino-3-ketobutyrate coenzyme A ligase [5] (data from MRSA252) SACOL0617 hexulose-6-phosphate synthase [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0876 hypothetical protein [5] (data from MRSA252) SACOL0914 FeS assembly ATPase SufC [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL1801 dipeptidase PepV [5] (data from MRSA252) SACOL1952 ferritins family protein [5] (data from MRSA252) SACOL2114 aldehyde dehydrogenase [5] (data from MRSA252) SACOL2163 hypothetical protein [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252) SACOL2296 glycerate dehydrogenase [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]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: 25.2 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 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)