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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02122
- pan locus tag?: SAUPAN004933000
- symbol: SAOUHSC_02122
- pan gene symbol?: ligA
- synonym:
- product: NAD-dependent DNA ligase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3921193 NCBI
- RefSeq: YP_500613 NCBI
- BioCyc: G1I0R-2009 BioCyc
- MicrobesOnline: 1290569 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1981ATGGCTGATTTATCGTCTCGTGTGAACGAGTTACATGATTTATTAAATCAATACAGTTAT
GAATACTATGTAGAGGATAATCCATCTGTACCAGATAGTGAATATGACAAATTACTTCAT
GAACTGATTAAAATAGAAGAGGAGCATCCTGAGTATAAGACTGTAGATTCTCCAACAGTT
AGAGTTGGCGGTGAAGCCCAAGCCTCTTTCAATAAAGTCAACCATGACACGCCAATGTTA
AGTTTAGGGAATGCATTTAATGAGGATGATTTGAGAAAATTCGACCAACGCATACGTGAA
CAAATTGGCAACGTTGAATATATGTGCGAATTAAAAATTGATGGCTTAGCAGTATCATTG
AAATATGTTGATGGATACTTCGTTCAAGGTTTAACACGTGGTGATGGAACAACAGGTGAA
GATATTACCGAAAATTTAAAAACAATTCATGCGATACCTTTGAAAATGAAAGAACCATTA
AATGTAGAAGTTCGTGGTGAAGCATATATGCCGAGACGTTCATTTTTACGATTAAATGAA
GAAAAAGAAAAAAATGATGAGCAGTTATTTGCAAATCCAAGAAACGCTGCTGCGGGATCA
TTAAGACAGTTAGATTCTAAATTAACGGCAAAACGAAAGCTAAGCGTATTTATATATAGT
GTCAATGATTTCACTGATTTCAATGCGCGTTCGCAAAGTGAAGCATTAGATGAGTTAGAT
AAATTAGGTTTTACAACGAATAAAAATAGAGCGCGTGTAAATAATATCGATGGTGTTTTA
GAGTATATTGAAAAATGGACAAGCCAAAGAGAGTCATTACCTTATGATATTGATGGGATT
GTTATTAAGGTTAATGATTTAGATCAACAGGATGAGATGGGATTCACACAAAAATCTCCT
AGATGGGCCATTGCTTATAAATTTCCAGCTGAGGAAGTAGTAACTAAATTATTAGATATT
GAATTAAGTATTGGACGAACAGGTGTAGTCACACCTACTGCTATTTTAGAACCAGTAAAA
GTAGCTGGTACAACTGTATCAAGAGCATCTTTGCACAATGAGGATTTAATTCATGACAGA
GATATTCGAATTGGTGATAGTGTTGTAGTGAAAAAAGCAGGTGACATCATACCTGAAGTT
GTACGTAGTATTCCAGAACGTAGACCTGAGGATGCTGTCACATATCATATGCCAACCCAT
TGTCCAAGTTGTGGACATGAATTAGTACGTATTGAAGGCGAAGTAGCACTTCGTTGCATT
AATCCAAAATGCCAAGCACAACTTGTTGAAGGATTGATTCACTTTGTATCAAGACAAGCC
ATGAATATTGATGGTTTAGGCACTAAAATTATTCAACAGCTTTATCAAAGCGAATTAATT
AAAGATGTTGCTGATATTTTCTATTTAACAGAAGAAGATTTATTACCTTTAGACAGAATG
GGGCAGAAAAAAGTTGATAATTTATTAGCTGCCATTCAACAAGCTAAGGACAACTCTTTA
GAAAATTTATTATTTGGTCTAGGTATTAGGCATTTAGGTGTTAAAGCGAGCCAAGTGTTA
GCAGAAAAATATGAAACGATAGATCGATTACTAACGGTAACTGAAGCGGAATTAGTAGAA
ATTCATGATATAGGTGATAAAGTAGCACAATCTGTAGTTACTTATTTAGAAAATGAAGAT
ATTCGTGCTTTAATTCAAAAATTAAAAGATAAACATGTTAATATGATTTATAAAGGTATC
AAAACATCAGATATTGAAGGACATCCTGAATTTAGTGGTAAAACGATAGTACTGACTGGT
AAGCTACATCAAATGACACGCAATGAAGCATCTAAATGGCTTGCATCACAAGGTGCTAAA
GTTACAAGTAGCGTTACTAAAAATACAGATGTCGTTATTGCTGGTGAAGATGCAGGTTCA
AAATTAACAAAAGCACAAAGTTTAGGTATTGAAATTTGGACAGAGCAACAATTTGTAGAT
AAGCAAAATGAATTAAATAGTTAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02122
- symbol: SAOUHSC_02122
- description: NAD-dependent DNA ligase
- length: 667
- theoretical pI: 4.90683
- theoretical MW: 75080.5
- GRAVY: -0.426087
⊟Function[edit | edit source]
- reaction: EC 6.5.1.2? ExPASyDNA ligase (NAD+) NAD+ + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta-nicotinamide D-nucleotide
- TIGRFAM: DNA metabolism DNA replication, recombination, and repair DNA ligase, NAD-dependent (TIGR00575; EC 6.5.1.2; HMM-score: 880.9)and 2 moreTranscription DNA-dependent RNA polymerase DNA-directed RNA polymerase, alpha subunit (TIGR02027; EC 2.7.7.6; HMM-score: 13.7)Protein fate Degradation of proteins, peptides, and glycopeptides zinc-dependent metalloproteinase lipoprotein, BF0631 family (TIGR03952; EC 3.4.24.-; HMM-score: 12.2)
- TheSEED :
- DNA ligase (EC 6.5.1.2)
- PFAM: DNA_ligase (CL0078) DNA_ligase_aden; NAD-dependent DNA ligase adenylation domain (PF01653; HMM-score: 438.3)and 12 moreOB (CL0021) DNA_ligase_OB; NAD-dependent DNA ligase OB-fold domain (PF03120; HMM-score: 115)HHH (CL0198) HHH_2; Helix-hairpin-helix motif (PF12826; HMM-score: 74.4)BRCT-like (CL0459) BRCT; BRCA1 C Terminus (BRCT) domain (PF00533; HMM-score: 50.9)no clan defined DNA_ligase_ZBD; NAD-dependent DNA ligase C4 zinc finger domain (PF03119; HMM-score: 42.8)HHH (CL0198) HHH_5; Helix-hairpin-helix domain (PF14520; HMM-score: 42.6)RNA_pol_A_CTD; Bacterial RNA polymerase, alpha chain C terminal domain (PF03118; HMM-score: 22)BRCT-like (CL0459) PTCB-BRCT; twin BRCT domain (PF12738; HMM-score: 21.5)Zn_Beta_Ribbon (CL0167) zf-NADH-PPase; NADH pyrophosphatase zinc ribbon domain (PF09297; HMM-score: 21.3)HHH (CL0198) HHH; Helix-hairpin-helix motif (PF00633; HMM-score: 14.7)Glyoxalase (CL0104) Glyoxalase_2; Glyoxalase-like domain (PF12681; HMM-score: 14)no clan defined zf-IS66; zinc-finger binding domain of transposase IS66 (PF13005; HMM-score: 12.9)zf-tcix; Putative treble-clef, zinc-finger, Zn-binding (PF14952; HMM-score: 11.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Mg2+, Mn2+
- 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): 0.003115
- TAT(Tat/SPI): 0.000545
- LIPO(Sec/SPII): 0.000491
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MADLSSRVNELHDLLNQYSYEYYVEDNPSVPDSEYDKLLHELIKIEEEHPEYKTVDSPTVRVGGEAQASFNKVNHDTPMLSLGNAFNEDDLRKFDQRIREQIGNVEYMCELKIDGLAVSLKYVDGYFVQGLTRGDGTTGEDITENLKTIHAIPLKMKEPLNVEVRGEAYMPRRSFLRLNEEKEKNDEQLFANPRNAAAGSLRQLDSKLTAKRKLSVFIYSVNDFTDFNARSQSEALDELDKLGFTTNKNRARVNNIDGVLEYIEKWTSQRESLPYDIDGIVIKVNDLDQQDEMGFTQKSPRWAIAYKFPAEEVVTKLLDIELSIGRTGVVTPTAILEPVKVAGTTVSRASLHNEDLIHDRDIRIGDSVVVKKAGDIIPEVVRSIPERRPEDAVTYHMPTHCPSCGHELVRIEGEVALRCINPKCQAQLVEGLIHFVSRQAMNIDGLGTKIIQQLYQSELIKDVADIFYLTEEDLLPLDRMGQKKVDNLLAAIQQAKDNSLENLLFGLGIRHLGVKASQVLAEKYETIDRLLTVTEAELVEIHDIGDKVAQSVVTYLENEDIRALIQKLKDKHVNMIYKGIKTSDIEGHPEFSGKTIVLTGKLHQMTRNEASKWLASQGAKVTSSVTKNTDVVIAGEDAGSKLTKAQSLGIEIWTEQQFVDKQNELNS
⊟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_00519 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [4] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [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_00524 (rpoB) DNA-directed RNA polymerase subunit beta [4] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_01250 (rpsO) 30S ribosomal protein S15 [4] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [4] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [4] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [4] (data from MRSA252) SAOUHSC_00006 DNA gyrase subunit A [4] (data from MRSA252) SAOUHSC_00069 protein A [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00196 hypothetical protein [4] (data from MRSA252) SAOUHSC_00469 regulatory protein SpoVG [4] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00871 D-alanine--poly(phosphoribitol) ligase subunit 2 [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_01041 pyruvate dehydrogenase complex, E1 component subunit beta [4] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [4] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01222 DNA topoisomerase I [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [4] (data from MRSA252) SAOUHSC_01577 hypothetical protein [4] (data from MRSA252) SAOUHSC_01797 DNA polymerase I [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01814 hypothetical protein [4] (data from MRSA252) SAOUHSC_01820 acetate kinase [4] (data from MRSA252) SAOUHSC_01879 virulence factor regulator protein [4] (data from MRSA252) SAOUHSC_02485 DNA-directed RNA polymerase subunit alpha [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252) SAOUHSC_02566 hypothetical protein [4] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_02121 < SAOUHSC_02122 < SAOUHSC_02123 < SAOUHSC_02124predicted SigA promoter [5] : SAOUHSC_02121 < SAOUHSC_02122 < SAOUHSC_02123 < SAOUHSC_02124 < SAOUHSC_02125 < S834 < SAOUHSC_02126 < S835
⊟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]
⊟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 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 4.46 4.47 4.48 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 5.2 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)