⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02536
- pan locus tag?: SAUPAN005729000
- symbol: SAOUHSC_02536
- pan gene symbol?: moaA
- synonym:
- product: molybdenum cofactor biosynthesis protein A
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_02536
- symbol: SAOUHSC_02536
- product: molybdenum cofactor biosynthesis protein A
- replicon: chromosome
- strand: -
- coordinates: 2336046..2337068
- length: 1023
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921126 NCBI
- RefSeq: YP_501000 NCBI
- BioCyc: G1I0R-2397 BioCyc
- MicrobesOnline: 1290971 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1021ATGGTAGAACAAATAAAAGATAAACTAGGACGTCCCATCCGTGACTTACGGTTATCTGTG
ACAGATCGGTGTAACTTTAGGTGTGATTATTGCATGCCTAAAGAGGTATTTGGAGATGAT
TTCGTATTTTTACCTAAAAATGAACTTTTAACGTTTGATGAAATGGCTAGAATCGCTAAG
GTATATGCAGAATTAGGTGTAAAAAAAATACGCATTACAGGTGGAGAACCATTGATGCGA
CGGGATTTAGATGTACTTATAGCTAAATTAAATCAAATCGATGGTATTGAAGATATTGGT
TTGACTACAAATGGTTTGTTATTAAAAAAGCATGGACAAAAGTTATATGATGCTGGGCTG
CGCAGAATTAATGTCAGTTTGGATGCTATTGATGATACGCTATTTCAATCAATCAATAAT
CGTAATATTAAAGCGACTACGATTTTAGAACAAATTGATTACGCGACGTCTATTGGTTTG
AATGTAAAAGTAAATGTTGTTATACAAAAAGGTATTAACGATGATCAAATCATACCAATG
CTTGAATATTTTAAAGATAAACATATAGAGATTCGATTTATAGAATTTATGGATGTTGGT
AATGATAATGGATGGGATTTCAGTAAAGTTGTAACTAAAGATGAAATGCTTACAATGATA
GAGCAGCACTTTGAAATCGATCCTGTAGAACCAAAATATTTTGGGGAAGTAGCAAAATAT
TATCGCCATAAGGATAATGGTGTTCAATTTGGTTTGATTACAAGTGTTTCACAATCATTT
TGTTCTACATGTACACGCGCAAGGCTGTCATCAGATGGGAAGTTTTACGGATGTTTATTT
GCAACTGTCGATGGATTTAACGTTAAAGCGTTTATTCGTTCTGGCGTGACCGACGAAGAA
TTAAAAGAACAATTTAAAGCTTTATGGCAAATAAGAGATGATCGATATTCAGATGAGAGA
ACTGCTCAAACAGTTGCCAATCGTCAACGTAAAAAGATAAACATGAATTATATTGGTGGT
TAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02536
- symbol: SAOUHSC_02536
- description: molybdenum cofactor biosynthesis protein A
- length: 340
- theoretical pI: 6.53074
- theoretical MW: 39077.6
- GRAVY: -0.343529
⊟Function[edit | edit source]
- ⊞reaction: EC 4.1.99.22? ExPASy
- ⊞TIGRFAM: Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor biosynthesis protein A (TIGR02666; HMM-score: 402.8)and 63 more
- TheSEED :
- GTP 3',8-cyclase (EC 4.1.99.22)
- ⊞PFAM: no clan defined Mob_synth_C; Molybdenum Cofactor Synthesis C (PF06463; HMM-score: 133.7)TIM_barrel (CL0036) Radical_SAM; Radical SAM superfamily (PF04055; HMM-score: 114.7)and 5 more
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: [4Fe-4S] cluster
- effectors:
⊟Localization[edit | edit source]
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MVEQIKDKLGRPIRDLRLSVTDRCNFRCDYCMPKEVFGDDFVFLPKNELLTFDEMARIAKVYAELGVKKIRITGGEPLMRRDLDVLIAKLNQIDGIEDIGLTTNGLLLKKHGQKLYDAGLRRINVSLDAIDDTLFQSINNRNIKATTILEQIDYATSIGLNVKVNVVIQKGINDDQIIPMLEYFKDKHIEIRFIEFMDVGNDNGWDFSKVVTKDEMLTMIEQHFEIDPVEPKYFGEVAKYYRHKDNGVQFGLITSVSQSFCSTCTRARLSSDGKFYGCLFATVDGFNVKAFIRSGVTDEELKEQFKALWQIRDDRYSDERTAQTVANRQRKKINMNYIGG
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell:
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_02536 < mobA < SAOUHSC_02538 < SAOUHSC_02540 < SAOUHSC_02541 < SAOUHSC_02542predicted SigA promoter [3] : SAOUHSC_02532 < S978 < SAOUHSC_02534 < SAOUHSC_02535 < S979 < SAOUHSC_02536 < mobA < SAOUHSC_02538 < SAOUHSC_02540 < SAOUHSC_02541 < SAOUHSC_02542 < S980 < SAOUHSC_02544 < SAOUHSC_02545 < S981 < SAOUHSC_02546 < SAOUHSC_02547 < SAOUHSC_02549
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [3] ⊟Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: no data available
⊞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]
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ Jump up to: 3.0 3.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)
⊟Relevant publications[edit | edit source]
Petra Hänzelmann, Hermann Schindelin
Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans.
Proc Natl Acad Sci U S A: 2004, 101(35);12870-5
[PubMed:15317939] [WorldCat.org] [DOI] (P p)Petra Hänzelmann, Hermann Schindelin
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism.
Proc Natl Acad Sci U S A: 2006, 103(18);6829-34
[PubMed:16632608] [WorldCat.org] [DOI] (P p)Nicholas S Lees, Petra Hänzelmann, Heather L Hernandez, Sowmya Subramanian, Hermann Schindelin, Michael K Johnson, Brian M Hoffman
ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications.
J Am Chem Soc: 2009, 131(26);9184-5
[PubMed:19566093] [WorldCat.org] [DOI] (I p)