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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02538
- pan locus tag?: SAUPAN005731000
- symbol: SAOUHSC_02538
- pan gene symbol?: moaD
- synonym:
- product: molybdopterin converting factor subunit 1
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3921128 NCBI
- RefSeq: YP_501002 NCBI
- BioCyc: G1I0R-2399 BioCyc
- MicrobesOnline: 1290973 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
61
121
181ATGAAGGTACTTTACTTCGCAGAAATTAAAGATATATTACAAAAAGCACAGGAAGATATT
GTGCTTGAACAAGCATTGACTGTACAACAATTTGAAGATTTATTGTTTGAACGTTATCCG
CAAATCAATAATAAAAAGTTTCAAGTTGCTGTAAATGAGGAATTTGTACAAAAATCGGAT
TTCATTCAACCTAATGATACTGTTGCATTAATTCCACCGGTTAGTGGAGGTTAA60
120
180
234
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02538
- symbol: SAOUHSC_02538
- description: molybdopterin converting factor subunit 1
- length: 77
- theoretical pI: 4.19545
- theoretical MW: 8871.09
- GRAVY: -0.172727
⊟Function[edit | edit source]
- TIGRFAM: Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdopterin converting factor, subunit 1 (TIGR01682; HMM-score: 76.7)and 2 moreBiosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin MoaD family protein (TIGR01687; HMM-score: 40.8)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiamine biosynthesis protein ThiS (TIGR01683; HMM-score: 16.2)
- TheSEED :
- Molybdopterin synthase sulfur carrier subunit
- PFAM: Ubiquitin (CL0072) ThiS; ThiS family (PF02597; HMM-score: 62.4)and 1 moreNADP_Rossmann (CL0063) UDPG_MGDP_dh_N; UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain (PF03721; HMM-score: 11.9)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: unknown (no significant prediction)
- Cytoplasmic Score: 2.5
- Cytoplasmic Membrane Score: 2.5
- Cellwall Score: 2.5
- Extracellular Score: 2.5
- 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): 0.00173
- TAT(Tat/SPI): 0.00019
- LIPO(Sec/SPII): 0.000286
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEDLLFERYPQINNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [2] [3]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [4] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [4] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00017 (rplI) 50S ribosomal protein L9 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [4] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [4] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_02501 (rplX) 50S ribosomal protein L24 [4] (data from MRSA252) SAOUHSC_02361 (rpmE2) 50S ribosomal protein L31 type B [4] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [4] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [4] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [4] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00634 ABC transporter substrate-binding protein [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01451 threonine dehydratase [4] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_02536 < mobA < SAOUHSC_02538 < SAOUHSC_02540 < SAOUHSC_02541 < SAOUHSC_02542predicted SigA promoter [5] : 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: [5] 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]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
BMC Genomics: 2009, 10;291
[PubMed:19570206] [WorldCat.org] [DOI] (I e) - ↑ 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) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 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) - ↑ 5.0 5.1 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)