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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
  • pan locus tag?: SAUPAN004200000
  • symbol: SACOL1661
  • pan gene symbol?: —
  • synonym:
  • product: acetyl-CoA carboxylase, biotin carboxylase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
  • symbol: SACOL1661
  • product: acetyl-CoA carboxylase, biotin carboxylase
  • replicon: chromosome
  • strand: -
  • coordinates: 1689999..1691360
  • length: 1362
  • 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
    ATGCTTCGTTGTTTAATTGCGAACAGAGGTGAAATTGCTGTAAGGATTATAAGAGCTTGC
    AGAGAATATGGGATTGAAACTGTAGCAGTTTATGCAAAAGGGGACGAGCAAAGCTTGCAT
    GTACATTTAGCAGATCAAGCTATATGTATTGGGGAAGCTAATGCTTTAGATAGTTATTTA
    AATATTGACCGCATCATATCTGCTGCACAAATCACTGGTGCTAATGCAATTCACCCAGGA
    TATGGCTTTTTATCAGAATCAACAAAATTTGCTCAAACCGTTGAGGAACAAGGCATAGCG
    TTTATAGGGCCTACTAAAAAAACGATGGAAATGATGGGGGATAAAATAACAGCAAGACAA
    ACAGTTCATCATGCAGGTGTTCCTGTGATTCCAGGATCAAATGGTGCTGTGAATCATGTG
    TCTGAAATTGAGAATCTTGCCAAAGACATCGGTTATCCAGTTGTTATCAAAGCTGCCAGT
    GGCGGTGGTGGTAAAGGTATACGTATTGTAAAGAAAGCTGAAGATTTAGAAAAGGCATTT
    AAAGAAGCTAAAAGTGAAGGAAAAAAATACTTTGATGATGATCGTGTTTATGTTGAGGCT
    TTTATACCTGTTGCAAAACATGTTGAAGTTCAAGTTATGGGAGATGGGCAGGATAATTAT
    GTACATTTAGGGGAACGTGATTGTTCTGTACAACGTAAAAATCAAAAATTAATCGAAGAA
    TCTCCTTGTGCAGCATTAACTGAAGAAAGACGACAACAAATATGTAACGATGCTGTTAAA
    GTTGCACGTGCAGCAAATTATAGAAGTGCAGGTACGATTGAATTTTTAGTAACTGATACC
    GCACATTACTTTATTGAAATGAATGCTCGAATACAAGTTGAACATACTGTTACAGAGATG
    CGAGCAGAACGTGATTTGGTTGCAGCACAACTGTATTTATTGGAACATAATCATTTACCT
    TTTTCACAAAGCGATATTCAATTTAATGGTCATGTGATAGAAGCGAGAATAAATGCCGAA
    AATCCTGAAAAGAAATTTCAACCAACACCAGGTAAAGTGACAGCGTTACATTTACCTCAA
    GGCTTTAATGTGCGAGTCGATTCTTTACTATATCACGGTTATCAAGTTTCACCATATTAT
    GATTCTTTAGTAGCTAAAGTAATTGTAAAATCTCATGATAGAGCTTCAGCAATTGATAAG
    TTGAAAGTCACCTTAGATGAAATGGTGATAGATGGATTTTCTACAACTGCCGATTTTTTA
    TATGCAGTTTTAAATTATCCACTATATCGTGATGGAGATGCAAAAGATGTTGATATTAAA
    TTTTTAGAAAAACATCAAATTGTTAAAGGGGTGGAATTATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1362

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
  • symbol: SACOL1661
  • description: acetyl-CoA carboxylase, biotin carboxylase
  • length: 453
  • theoretical pI: 6.36863
  • theoretical MW: 50223.8
  • GRAVY: -0.237086

⊟Function[edit | edit source]

  • ⊞TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 601.9)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 508.4)
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 502.1)
    and 11 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, large subunit (TIGR01369; EC 6.3.5.5; HMM-score: 56.1)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan D-alanine--D-alanine ligase (TIGR01205; EC 6.3.2.4; HMM-score: 54.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylglycinamide formyltransferase 2 (TIGR01142; EC 2.1.2.-; HMM-score: 49.5)
    Cellular processes Cellular processes Biosynthesis of natural products cyanophycin synthetase (TIGR02068; EC 6.3.2.29,6.3.2.30; HMM-score: 47.5)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazole carboxylase, ATPase subunit (TIGR01161; EC 4.1.1.21; HMM-score: 43.3)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylamine--glycine ligase (TIGR00877; EC 6.3.4.13; HMM-score: 40.4)
    alpha-L-glutamate ligase, RimK family (TIGR00768; EC 6.3.2.-; HMM-score: 37.8)
    lysine biosynthesis enzyme LysX (TIGR02144; HMM-score: 36.1)
    alpha-L-glutamate ligase homolog (TIGR02291; HMM-score: 18.9)
    Metabolism Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylC (TIGR03909; HMM-score: 16.1)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other coenzyme gamma-F420-2:alpha-L-glutamate ligase (TIGR04443; EC 6.3.2.32; HMM-score: 13.6)
  • TheSEED  :
    • Biotin carboxylase (EC 6.3.4.14)
    Allophanate hydrolase 2 and Biotin carboxylase cluster  Biotin carboxylase (EC 6.3.4.14)
  • ⊞PFAM:
    ATP-grasp (CL0179) CPSase_L_D2; Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786; HMM-score: 215.6)
    and 13 more
    NADP_Rossmann (CL0063) Biotin_carb_N; Biotin carboxylase, N-terminal domain (PF00289; HMM-score: 153.6)
    Hybrid (CL0105) Biotin_carb_C; Biotin carboxylase C-terminal domain (PF02785; HMM-score: 122.4)
    ATP-grasp (CL0179) Dala_Dala_lig_C; D-ala D-ala ligase C-terminus (PF07478; HMM-score: 48)
    ATP-grasp; ATP-grasp domain (PF02222; HMM-score: 42.4)
    ATP-grasp_3; ATP-grasp domain (PF02655; HMM-score: 32.8)
    ATPgrasp_ST; Sugar-transfer associated ATP-grasp (PF14397; HMM-score: 28.2)
    RimK; RimK-like ATP-grasp domain (PF08443; HMM-score: 21.9)
    GARS_A; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain (PF01071; HMM-score: 20.8)
    ATP-grasp_4; ATP-grasp domain (PF13535; HMM-score: 19.9)
    ATP-grasp_5; ATP-grasp domain (PF13549; HMM-score: 15.1)
    ATPgrasp_TupA; TupA-like ATPgrasp (PF14305; HMM-score: 12.7)
    no clan defined DUF3906; Protein of unknown function (DUF3906) (PF13046; HMM-score: 12.4)
    P-loop_NTPase (CL0023) DEAD; DEAD/DEAH box helicase (PF00270; HMM-score: 12)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • 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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.978
    • Cytoplasmic Membrane Score: 0.009
    • Cell wall & surface Score: 0.0003
    • Extracellular Score: 0.0127
  • ⊞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): 0.010201
    • TAT(Tat/SPI): 0.000437
    • LIPO(Sec/SPII): 0.005396
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MLRCLIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFLSESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIENLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDTAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKVTLDEMVIDGFSTTADFLYAVLNYPLYRDGDAKDVDIKFLEKHQIVKGVEL

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 27 [4]
  • ⊟interaction partners:
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [5] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [5] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [5] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [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)
    SACOL0018(purA)adenylosuccinate synthetase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • ⊞regulator: CcpA regulon

⊟Transcription pattern[edit | edit source]

⊟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]

  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. ↑ Jump up to: 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 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)

⊟Relevant publications[edit | edit source]

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