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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1965 [new locus tag: SACOL_RS10275 ]
  • pan locus tag?: SAUPAN004933000
  • symbol: ligA
  • pan gene symbol?: ligA
  • synonym:
  • product: DNA ligase, NAD-dependent

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1965 [new locus tag: SACOL_RS10275 ]
  • symbol: ligA
  • product: DNA ligase, NAD-dependent
  • replicon: chromosome
  • strand: -
  • coordinates: 2026692..2028695
  • length: 2004
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟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
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    1681
    1741
    1801
    1861
    1921
    1981
    ATGGCTGATTTATCGTCTCGTGTGAACGAGTTACATGATTTATTAAATCAATACAGTTAT
    GAATACTATGTAGAGGATAATCCATCTGTACCAGATAGTGAATATGACAAATTACTTCAT
    GAACTGATTAAAATAGAAGAGGAGCATCCTGAGTATAAGACTGTAGATTCTCCAACAGTT
    AGAGTTGGCGGTGAAGCCCAAGCCTCTTTCAATAAAGTCAACCATGACACGCCAATGTTA
    AGTTTAGGGAATGCATTTAATGAGGATGATTTGAGAAAATTCGACCAACGCATACGTGAA
    CAAATTGGCAACGTTGAATATATGTGCGAATTAAAAATTGATGGCTTAGCAGTATCATTG
    AAATATGTTGATGGATACTTCGTTCAAGGTTTAACACGTGGTGATGGAACAACAGGTGAA
    GATATTACCGAAAATTTAAAAACAATTCATGCGATACCTTTGAAAATGAAAGAACCATTA
    AATGTAGAAGTTCGTGGTGAAGCATATATGCCGAGACGTTCATTTTTACGATTAAATGAA
    GAAAAAGAAAAAAATGATGAGCAGTTATTTGCAAATCCAAGAAACGCTGCTGCGGGATCA
    TTAAGACAGTTAGATTCTAAATTAACGGCAAAACGAAAGCTAAGCGTATTTATATATAGT
    GTCAATGATTTCACTGATTTCAATGCGCGTTCGCAAAGTGAAGCATTAGATGAGTTAAAT
    AAATTAGGTTTTACAACGAATAAAAATAGAGCGCGTGTAAATAATATCGATGGTGTTTTA
    GAGTATATTGAAAAATGGACAAGCCAAAGAGAGTCATTACCTTATGATATTGATGGGATT
    GTTATTAAGGTTAATGATTTAGATCAACAGGATGAGATGGGATTCACACAAAAATCTCCT
    AGATGGGCCATTGCTTATAAATTTCCAGCTGAGGAAGTAGTAACTAAATTATTAGATATT
    GAATTAAGTATTGGACGAACAGGTGTAGTCACACCTACTGCTATTTTAGAACCAGTAAAA
    GTAGCTGGTACAACTGTATCAAGAGCATCTTTGCACAATGAGGATTTAATTCATGACAGA
    GATATTCGAATTGGTGATAGTGTTGTAGTGAAAAAAGCAGGTGACATCATACCTGAAGTT
    GTACGTAGTATTCCAGAACGTAGACCTGAGGATGCTGTCACATATCATATGCCAACCCAT
    TGTCCAAGTTGTGGACATGAATTAGTACGTATTGAAGGCGAAGTAGCACTTCGTTGCATT
    AATCCAAAATGCCAAGCACAACTTGTTGAAGGATTGATTCACTTTGTATCAAGACAAGCC
    ATGAATATTGATGGTTTAGGCACTAAAATTATTCAACAGCTTTATCAAAGCGAATTAATT
    AAAGATGTTGCTGATATTTTCTATTTAACAGAAGAAGATTTATTACCTTTAGACAGAATG
    GGGCAGAAAAAAGTTGATAATTTATTAGCTGCCATTCAACAAGCTAAGGACAACTCTTTA
    GAAAATTTATTATTTGGTCTAGGTATTAGGCATTTAGGTGTTAAAGCGAGCCAAGTGTTA
    GCAGAAAAATATGAAACGATAGATCGATTACTAACGGTAACTGAAGCGGAATTAGTAGAA
    ATTCATGATATAGGTGATAAAGTAGCACAATCTGTAGTTACTTATTTAGAAAATGAAGAT
    ATTCGTGCTTTAATTCAAAAATTAAAAGATAAACATGTTAATATGATTTATAAAGGTATC
    AAAACATCAGATATTGAAGGACATCCTGAATTTAGTGGTAAAACGATAGTACTGACTGGT
    AAGCTACATCAAATGACACGCAATGAAGCATCTAAATGGCTTGCATCACAAGGTGCTAAA
    GTTACAAGTAGCGTTACTAAAAATACAGATGTCGTTATTGCTGGTGAAGATGCAGGTTCA
    AAATTAACAAAAGCACAAAGTTTAGGTATTGAAATTTGGACAGAGCAACAATTTGTAGAT
    AAGCAAAATGAATTAAATAGTTAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740
    1800
    1860
    1920
    1980
    2004

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1965 [new locus tag: SACOL_RS10275 ]
  • symbol: LigA
  • description: DNA ligase, NAD-dependent
  • length: 667
  • theoretical pI: 4.94308
  • theoretical MW: 75079.5
  • GRAVY: -0.426087

⊟Function[edit | edit source]

  • reaction:
    EC 6.5.1.2?  ExPASy
    DNA ligase (NAD+) NAD+ + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta-nicotinamide D-nucleotide
  • TIGRFAM:
    Genetic information processing DNA metabolism DNA replication, recombination, and repair DNA ligase, NAD-dependent (TIGR00575; EC 6.5.1.2; HMM-score: 880.9)
    and 2 more
    Genetic information processing Transcription DNA-dependent RNA polymerase DNA-directed RNA polymerase, alpha subunit (TIGR02027; EC 2.7.7.6; HMM-score: 13.8)
    Genetic information processing 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)
    DNA Metabolism DNA repair DNA Repair Base Excision  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 more
    OB (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]

  • MADLSSRVNELHDLLNQYSYEYYVEDNPSVPDSEYDKLLHELIKIEEEHPEYKTVDSPTVRVGGEAQASFNKVNHDTPMLSLGNAFNEDDLRKFDQRIREQIGNVEYMCELKIDGLAVSLKYVDGYFVQGLTRGDGTTGEDITENLKTIHAIPLKMKEPLNVEVRGEAYMPRRSFLRLNEEKEKNDEQLFANPRNAAAGSLRQLDSKLTAKRKLSVFIYSVNDFTDFNARSQSEALDELNKLGFTTNKNRARVNNIDGVLEYIEKWTSQRESLPYDIDGIVIKVNDLDQQDEMGFTQKSPRWAIAYKFPAEEVVTKLLDIELSIGRTGVVTPTAILEPVKVAGTTVSRASLHNEDLIHDRDIRIGDSVVVKKAGDIIPEVVRSIPERRPEDAVTYHMPTHCPSCGHELVRIEGEVALRCINPKCQAQLVEGLIHFVSRQAMNIDGLGTKIIQQLYQSELIKDVADIFYLTEEDLLPLDRMGQKKVDNLLAAIQQAKDNSLENLLFGLGIRHLGVKASQVLAEKYETIDRLLTVTEAELVEIHDIGDKVAQSVVTYLENEDIRALIQKLKDKHVNMIYKGIKTSDIEGHPEFSGKTIVLTGKLHQMTRNEASKWLASQGAKVTSSVTKNTDVVIAGEDAGSKLTKAQSLGIEIWTEQQFVDKQNELNS

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 233 [4]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL0937(dltC)D-alanine--poly(phosphoribitol) ligase subunit 2  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0006(gyrA)DNA gyrase, A subunit  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [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)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL1737(polA)DNA polymerase I  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL1812(rot)repressor of toxins  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [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)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL2287(sarR)accessory regulator R  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL0541(spoVG)regulatory protein SpoVG  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL1267(topA)DNA topoisomerase I  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 36.22 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]

  1. ↑ 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)
  2. ↑ 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)
  3. ↑ 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)
  4. ↑ 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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 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)
  6. ↑ 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)

⊟Relevant publications[edit | edit source]

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