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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01688
- pan locus tag?: SAUPAN004171000
- symbol: SAOUHSC_01688
- pan gene symbol?: lepA
- synonym:
- product: GTP-binding protein LepA
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01688
- symbol: SAOUHSC_01688
- product: GTP-binding protein LepA
- replicon: chromosome
- strand: -
- coordinates: 1597937..1599760
- length: 1824
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921800 NCBI
- RefSeq: YP_500198 NCBI
- BioCyc: G1I0R-1569 BioCyc
- MicrobesOnline: 1290112 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1801ATGGATAATGAGCAACGCTTAAAAAGAAGAGAGAATATAAGGAATTTCTCGATTATAGCA
CATATTGACCACGGAAAATCTACATTGGCTGATAGAATTTTAGAAAATACCAAATCAGTT
GAAACAAGAGATATGCAAGATCAGTTACTAGATTCAATGGATTTAGAAAGAGAACGTGGT
ATTACAATCAAATTAAACGCAGTACGTTTAAAGTACGAAGCTAAAGATGGAAATACTTAT
ACATTCCATTTAATCGATACGCCTGGACACGTCGATTTTACATATGAAGTGTCACGTTCT
TTGGCAGCTTGTGAGGGCGCGATTTTAGTAGTAGATGCGGCTCAAGGTATCGAAGCACAA
ACATTAGCAAATGTTTATTTAGCATTAGATAATGAGTTAGAGTTATTGCCTGTTATTAAC
AAAATTGATTTACCTGCTGCAGAACCTGAACGCGTGAAACAAGAAATTGAAGATATGATA
GGTTTAGACCAAGACGATGTTGTTTTAGCAAGTGCTAAATCTAACATTGGAATTGAAGAG
ATACTAGAGAAAATAGTTGAAGTTGTGCCAGCTCCAGATGGTGACCCAGAAGCACCACTA
AAAGCGTTAATATTTGATTCTGAGTATGATCCATATAGAGGGGTAATTTCATCGATAAGA
ATTGTGGACGGTGTTGTTAAAGCCGGAGATAAAATTCGAATGATGGCCACTGGTAAAGAG
TTCGAAGTAACAGAAGTTGGAATTAATACACCTAAGCAGCTTCCAGTTGATGAATTAACA
GTTGGTGATGTTGGTTATATTATTGCAAGTATTAAAAATGTTGATGATTCTAGGGTTGGT
GACACCATCACATTAGCTAGTAGACCTGCATCAGAACCATTGCAAGGTTATAAGAAAATG
AATCCAATGGTATATTGCGGACTGTTCCCAATAGATAACAAAAATTATAATGATTTAAGA
GAAGCATTAGAAAAATTACAATTGAATGATGCATCATTAGAATTTGAGCCTGAATCGTCA
CAAGCATTAGGTTTTGGTTATAGAACTGGTTTCTTAGGTATGTTACACATGGAAATAATT
CAAGAAAGAATTGAAAGAGAATTTGGTATTGAATTAATTGCAACTGCACCATCTGTAATT
TATCAATGTGTTTTAAGGGACGGTTCAGAAGTGACGGTTGATAACCCAGCACAAATGCCA
GATCGTGATAAAATTGATAAAATATTTGAGCCATATGTTCGTGCAACTATGATGGTTCCA
AATGACTATGTCGGTGCAGTAATGGAATTATGTCAACGTAAACGTGGACAATTTATAAAT
ATGGACTATTTAGATGATATTCGTGTAAATATTGTTTATGAATTACCTTTAGCTGAAGTT
GTATTTGATTTCTTCGATCAACTTAAATCTAATACTAAAGGATATGCATCATTTGATTAT
GAATTCATCGAAAATAAAGAAAGTAATTTAGTCAAGATGGATATTTTATTAAATGGTGAT
AAAGTGGATGCGCTAAGCTTCATAGTTCATAGAGATTTTGCATATGAACGTGGTAAAGCA
TTAGTTGAAAAACTTAAAACGTTAATTCCAAGACAGCAATTTGAAGTACCTGTACAGGCT
GCAATAGGACAAAAAATTGTAGCGCGTACAAATATTAAATCAATGGGTAAAAACGTTTTA
GCTAAATGTTATGGCGGTGACATAAGCCGTAAACGTAAATTACTTGAAAAACAAAAAGCA
GGTAAAGCTAAGATGAAAGCAGTTGGTAATGTTGAAATTCCACAAGATGCTTTCTTGGCT
GTATTGAAAATGGATGATGAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01688
- symbol: SAOUHSC_01688
- description: GTP-binding protein LepA
- length: 607
- theoretical pI: 4.59347
- theoretical MW: 68174.6
- GRAVY: -0.259473
⊟Function[edit | edit source]
- reaction: EC 3.6.5.n1? ExPASyElongation factor 4 GTP + H2O = GDP + phosphate
- TIGRFAM: Unknown function General elongation factor 4 (TIGR01393; EC 3.6.5.-; HMM-score: 1014.8)and 20 moreCellular processes Adaptations to atypical conditions GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 216.6)Protein synthesis Translation factors GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 216.6)Regulatory functions Other GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 216.6)Protein synthesis Translation factors translation elongation factor G (TIGR00484; HMM-score: 199.5)Protein synthesis Translation factors translation elongation factor aEF-2 (TIGR00490; HMM-score: 179.8)Protein synthesis Translation factors peptide chain release factor 3 (TIGR00503; HMM-score: 98.5)Protein synthesis Translation factors translation initiation factor IF-2 (TIGR00487; HMM-score: 87.1)Protein synthesis Translation factors translation elongation factor Tu (TIGR00485; HMM-score: 74.3)Unknown function General small GTP-binding protein domain (TIGR00231; HMM-score: 72)Protein synthesis Translation factors selenocysteine-specific translation elongation factor (TIGR00475; HMM-score: 68.1)Protein synthesis Translation factors translation elongation factor EF-1, subunit alpha (TIGR00483; HMM-score: 56.4)Central intermediary metabolism Sulfur metabolism sulfate adenylyltransferase, large subunit (TIGR02034; EC 2.7.7.4; HMM-score: 54.7)translation initiation factor 2, gamma subunit (TIGR03680; HMM-score: 42.8)Protein synthesis Translation factors translation initiation factor aIF-2 (TIGR00491; HMM-score: 36.9)Protein synthesis Other ribosome-associated GTPase EngA (TIGR03594; HMM-score: 33.9)Protein fate Protein modification and repair [FeFe] hydrogenase H-cluster maturation GTPase HydF (TIGR03918; HMM-score: 20.2)Unknown function General GTP-binding protein HflX (TIGR03156; HMM-score: 19.1)Energy metabolism Amino acids and amines ethanolamine utilization protein, EutP (TIGR02528; HMM-score: 18.8)Protein synthesis Other ribosome biogenesis GTPase YqeH (TIGR03597; HMM-score: 17.2)Protein synthesis Other ribosome biogenesis GTP-binding protein YsxC (TIGR03598; HMM-score: 16)
- TheSEED :
- Translation elongation factor LepA
Protein Metabolism Protein biosynthesis Translation elongation factors bacterial Translation elongation factor LepAand 2 more - PFAM: P-loop_NTPase (CL0023) GTP_EFTU; Elongation factor Tu GTP binding domain (PF00009; HMM-score: 181.8)no clan defined LepA_C; GTP-binding protein LepA C-terminus (PF06421; HMM-score: 166.3)and 10 moreEF-G_C (CL0437) EFG_C; Elongation factor G C-terminus (PF00679; HMM-score: 82.8)EFTPs (CL0575) GTP_EFTU_D2; Elongation factor Tu domain 2 (PF03144; HMM-score: 51.6)EF-G_C (CL0437) EFG_II; Elongation Factor G, domain II (PF14492; HMM-score: 25.6)P-loop_NTPase (CL0023) MMR_HSR1; 50S ribosome-binding GTPase (PF01926; HMM-score: 23.2)Ras; Ras family (PF00071; HMM-score: 19.3)SRPRB; Signal recognition particle receptor beta subunit (PF09439; HMM-score: 16.2)PduV-EutP; Ethanolamine utilisation - propanediol utilisation (PF10662; HMM-score: 15.6)no clan defined MMR_HSR1_Xtn; C-terminal region of MMR_HSR1 domain (PF16897; HMM-score: 15.6)Adeno_E3_15_3; Adenovirus 15.3kD protein in E3 region (PF03307; HMM-score: 15.5)EF-G_C (CL0437) RF3_C; Class II release factor RF3, C-terminal domain (PF16658; HMM-score: 15.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic Membrane
- Cytoplasmic Score: 1.05
- Cytoplasmic Membrane Score: 8.78
- Cellwall Score: 0.08
- Extracellular Score: 0.09
- 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): 0.005084
- TAT(Tat/SPI): 0.000787
- LIPO(Sec/SPII): 0.000635
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MDNEQRLKRRENIRNFSIIAHIDHGKSTLADRILENTKSVETRDMQDQLLDSMDLERERGITIKLNAVRLKYEAKDGNTYTFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNELELLPVINKIDLPAAEPERVKQEIEDMIGLDQDDVVLASAKSNIGIEEILEKIVEVVPAPDGDPEAPLKALIFDSEYDPYRGVISSIRIVDGVVKAGDKIRMMATGKEFEVTEVGINTPKQLPVDELTVGDVGYIIASIKNVDDSRVGDTITLASRPASEPLQGYKKMNPMVYCGLFPIDNKNYNDLREALEKLQLNDASLEFEPESSQALGFGYRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYQCVLRDGSEVTVDNPAQMPDRDKIDKIFEPYVRATMMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIVYELPLAEVVFDFFDQLKSNTKGYASFDYEFIENKESNLVKMDILLNGDKVDALSFIVHRDFAYERGKALVEKLKTLIPRQQFEVPVQAAIGQKIVARTNIKSMGKNVLAKCYGGDISRKRKLLEKQKAGKAKMKAVGNVEIPQDAFLAVLKMDDE
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01170 (carB) carbamoyl phosphate synthase large subunit [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_02116 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [3] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SAOUHSC_01262 (recA) recombinase A [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02505 (rplP) 50S ribosomal protein L16 [3] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_02361 (rpmE2) 50S ribosomal protein L31 type B [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_00527 (rpsL) 30S ribosomal protein S12 [3] (data from MRSA252) SAOUHSC_02487 (rpsM) 30S ribosomal protein S13 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_02353 (upp) uracil phosphoribosyltransferase [3] (data from MRSA252) SAOUHSC_00153 indolepyruvate decarboxylase [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00467 pur operon repressor [3] (data from MRSA252) SAOUHSC_00472 ribose-phosphate pyrophosphokinase [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01149 cell division protein [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01154 hypothetical protein [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01857 hypothetical protein [3] (data from MRSA252) SAOUHSC_02363 aldehyde dehydrogenase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- predicted SigA promoter [4] : SAOUHSC_01686 < S667 < SAOUHSC_01687 < S668 < SAOUHSC_01688 < S669
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] 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]
- ↑ 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) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 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) - ↑ 4.0 4.1 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]
Jerry R Colca, William G McDonald, Daniel J Waldon, Lisa M Thomasco, Robert C Gadwood, Eric T Lund, Gregory S Cavey, W Rodney Mathews, Lonnie D Adams, Eric T Cecil, James D Pearson, Jeffrey H Bock, John E Mott, Dean L Shinabarger, Liqun Xiong, Alexander S Mankin
Cross-linking in the living cell locates the site of action of oxazolidinone antibiotics.
J Biol Chem: 2003, 278(24);21972-9
[PubMed:12690106] [WorldCat.org] [DOI] (P p)