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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1215 [new locus tag: SACOL_RS06225 ]
  • pan locus tag?: SAUPAN003483000
  • symbol: carB
  • pan gene symbol?: carB
  • synonym:
  • product: carbamoyl phosphate synthase large subunit

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1215 [new locus tag: SACOL_RS06225 ]
  • symbol: carB
  • product: carbamoyl phosphate synthase large subunit
  • replicon: chromosome
  • strand: +
  • coordinates: 1222716..1225889
  • length: 3174
  • 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
    2041
    2101
    2161
    2221
    2281
    2341
    2401
    2461
    2521
    2581
    2641
    2701
    2761
    2821
    2881
    2941
    3001
    3061
    3121
    ATGCCTAAACGTAATGATATCAAAACAATTTTAGTAATAGGGTCTGGGCCAATTATCATA
    GGTCAAGCAGCTGAATTTGATTATGCTGGAACACAAGCATGTCTAGCTTTAAAAGAAGAG
    GGATATCGAGTTATTCTTGTAAATTCAAATCCAGCGACAATCATGACTGATAAGGAAATT
    GCGGATAAAGTATATATCGAACCGTTAACTCATGATTTTATAGCGCGAATTATACGTAAA
    GAGCAACCTGACGCTTTACTTCCAACTTTAGGTGGTCAAACAGGTTTAAACATGGCGATT
    CAACTACACGAAAGTGGTGTGCTTCAAGATAATAACGTCCAATTATTAGGAACTGAGCTA
    ACATCAATTCAACAAGCAGAAGACCGTGAAATGTTTAGAACATTAATGAATGATTTAAAC
    GTTCCTGTACCAGAGAGTGACATTGTAAATACAGTAGAGCAAGCCTTTAAATTCAAAGAG
    CAAGTGGGATACCCGCTAATTGTTAGACCGGCATTTACGATGGGTGGTACCGGAGGCGGT
    ATTTGTCATAATGATGAAGAATTACATGAAATCGTCTCAAATGGTCTTCATTATAGTCCA
    GCAACGCAATGTTTATTAGAAAAATCTATCGCAGGTTTTAAAGAAATCGAATACGAAGTA
    ATGCGTGATAAAAACGATAATGCCATCGTTGTATGTAACATGGAAAATATTGATCCAGTT
    GGTATTCATACAGGCGATTCAATTGTTGTGGCTCCTAGTCAAACATTATCAGATGTTGAG
    TATCAAATGTTACGTGATGTTTCATTAAAAGTTATTCGAGCTTTAGGTATCGAAGGTGGT
    TGTAATGTTCAATTAGCATTAGATCCCCATTCATTCGATTATTATATTATAGAAGTAAAT
    CCGCGTGTATCACGTTCATCAGCGTTAGCTTCAAAAGCAACAGGATATCCTATTGCAAAA
    TTAGCTGCTAAAATCGCGGTTGGTCTAACATTAGATGAAATGTTAAATCCAATTACAGGA
    ACATCTTATGCAGCGTTTGAACCAACTTTAGACTATGTGATTTCAAAAATACCAAGATTT
    CCTTTTGATAAATTTGAAAAAGGAGAACGAGAGCTTGGCACACAAATGAAAGCAACAGGT
    GAAGTTATGGCCATTGGTCGAACTTACGAAGAATCATTGTTAAAAGCAATTCGATCACTT
    GAGTATGGTGTGCATCACTTAGGATTACCAAATGGTGAAAGCTTCGATCTTGATTATATT
    AAAGAACGTATTTCACACCAAGATGATGAACGATTATTTTTCATCGGCGAAGCAATTAGA
    AGAGGCACAACATTAGAAGAAATTCATAATATGACTCAGATTGATTACTTCTTCTTACAC
    AAGTTCCAAAACATTATTGATATTGAGCATCAATTAAAAGAGCATCAAGGTGATTTAGAA
    TATCTTAAATATGCAAAAGATTATGGATTTAGTGATAAAACAATAGCGCATCGCTTTAAT
    ATGACGGAAGAAGAAGTATATCAATTGCGTATGGAAAATGATATTAAACCTGTTTACAAG
    ATGGTTGATACTTGCGCAGCTGAATTTGAATCTTCAACACCATATTATTATGGTACATAC
    GAAACTGAAAATGAATCCATAGTTACTGACAAAGAAAAAATCTTAGTATTAGGCTCTGGA
    CCAATTCGAATCGGCCAAGGTGTAGAATTTGACTATGCGACAGTTCATGCCGTTTGGGCA
    ATTCAAAAAGCAGGGTACGAAGCGATAATTGTGAATAACAATCCAGAAACAGTTTCAACA
    GACTTCTCAATTTCTGACAAATTATACTTTGAACCTTTAACTGAAGAAGATGTGATGAAT
    ATCATTAATTTAGAAAAACCTAAAGGTGTCGTTGTACAATTTGGAGGACAAACAGCGATT
    AATTTAGCAGACAAATTGGCTAAACATGGTGTTAAAATACTTGGTACTTCACTAGAAAAT
    CTAAATCGTGCTGAAGATAGAAAAGAATTTGAAGCACTATTAAGAAAAATTAACGTGCCA
    CAGCCACAAGGGAAAACAGCTACATCACCTGAGGAAGCATTAGCGAATGCTGCAGAAATC
    GGATATCCGGTTGTAGTAAGACCTTCTTATGTATTAGGTGGTCGCGCAATGGAAATTGTA
    GACAATGACAAAGAGTTAGAAAACTATATGACCCAGGCTGTAAAAGCGAGTCCGGAACAT
    CCGGTACTAGTCGATAGATATTTAACTGGTAAAGAAATTGAAGTTGATGCGATTTGTGAT
    GGAGAAACGGTCATTATTCCAGGAATCATGGAACATATTGAACGTGCTGGTGTGCATAGT
    GGTGACTCAATCGCTGTATATCCACCACAAACTTTGACAGAAGACGAGTTAGCAACACTT
    GAGGACTATACTATAAAATTAGCTAAAGGTTTAAACATCATTGGCTTAATCAACATTCAA
    TTCGTTATAGCTCACGATGGTGTGTATGTTTTAGAAGTAAATCCACGTTCTAGTAGAACG
    GTACCATTCTTAAGTAAAATTACTGATATTCCAATGGCACAATTAGCTATGCGAGCAATC
    ATTGGGGAAAAACTAACAGATATGGGTTATCAAGAAGGGGTTCAACCATATGCTGAGGGT
    GTCTTTGTGAAAGCACCAGTATTTAGTTTTAATAAATTGAAAAATGTTGATATTACTTTA
    GGACCTGAAATGAAGTCAACAGGTGAAGTGATGGGGAAAGATACTACATTAGAAAAGGCG
    TTATTCAAAGGGTTAACAGGTAGTGGCGTTGAAGTTAAAGATCACGGTACAGTATTAATG
    ACCGTCAGTGACAAAGATAAAGAGGAAGTTGTTAAATTGGCACAACGCTTAAATGAAGTT
    GGCTATAAAATTTTAGCAACGTCTGGAACAGCTAATAAATTAGCTGAGTATGACATACCT
    GCAGAAGTAGTAGGCAAAATTGGTGGCGAAAATGATTTATTAACACGTATTCAAAATGGT
    GATGTTCAAATCGTTATAAATACAATGACTAAAGGTAAAGAAGTAGAAAGGGATGGCTTC
    CAAATTAGACGTACTACAGTTGAAAATGGTATTCCATGTTTGACATCTTTAGATACAGCT
    AATGCCTTAACGAATGTAATTGAAAGTATGACATTTACAATGCGTCAAATGTAA
    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
    2040
    2100
    2160
    2220
    2280
    2340
    2400
    2460
    2520
    2580
    2640
    2700
    2760
    2820
    2880
    2940
    3000
    3060
    3120
    3174

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1215 [new locus tag: SACOL_RS06225 ]
  • symbol: CarB
  • description: carbamoyl phosphate synthase large subunit
  • length: 1057
  • theoretical pI: 4.60041
  • theoretical MW: 117185
  • GRAVY: -0.194229

⊟Function[edit | edit source]

  • reaction:
    EC 6.3.5.5?  ExPASy
    Carbamoyl-phosphate synthase (glutamine-hydrolyzing) 2 ATP + L-glutamine + HCO3(-) + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, large subunit (TIGR01369; EC 6.3.5.5; HMM-score: 1581.7)
    and 15 more
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 128)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 99.8)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylglycinamide formyltransferase 2 (TIGR01142; EC 2.1.2.-; HMM-score: 96.2)
    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: 91.7)
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 81.9)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylamine--glycine ligase (TIGR00877; EC 6.3.4.13; HMM-score: 74.7)
    lysine biosynthesis enzyme LysX (TIGR02144; HMM-score: 68.1)
    Cellular processes Cellular processes Biosynthesis of natural products cyanophycin synthetase (TIGR02068; EC 6.3.2.29,6.3.2.30; HMM-score: 67.6)
    Metabolism Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylC (TIGR03909; HMM-score: 66.4)
    alpha-L-glutamate ligase, RimK family (TIGR00768; EC 6.3.2.-; HMM-score: 57.8)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazole carboxylase, ATPase subunit (TIGR01161; EC 4.1.1.21; HMM-score: 52.1)
    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: 35.6)
    ATP-grasp enzyme, GAK system (TIGR04356; HMM-score: 27.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (TIGR00355; EC 2.1.2.3,3.5.4.10; HMM-score: 21.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin putative heme d1 biosynthesis radical SAM protein NirJ2 (TIGR04055; EC 1.3.99.-; HMM-score: 13.8)
  • TheSEED  :
    • Carbamoyl-phosphate synthase large chain (EC 6.3.5.5)
    Nucleosides and Nucleotides Pyrimidines De Novo Pyrimidine Synthesis  Carbamoyl-phosphate synthase large chain (EC 6.3.5.5)
  • PFAM:
    ATP-grasp (CL0179) CPSase_L_D2; Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786; HMM-score: 404.7)
    and 13 more
    no clan defined CPSase_L_D3; Carbamoyl-phosphate synthetase large chain, oligomerisation domain (PF02787; HMM-score: 139.6)
    ATP-grasp (CL0179) ATPgrasp_Ter; ATP-grasp in the biosynthetic pathway with Ter operon (PF15632; HMM-score: 96.9)
    no clan defined MGS; MGS-like domain (PF02142; HMM-score: 75.1)
    ATP-grasp (CL0179) ATP-grasp_3; ATP-grasp domain (PF02655; HMM-score: 73.5)
    Dala_Dala_lig_C; D-ala D-ala ligase C-terminus (PF07478; HMM-score: 67.1)
    ATP-grasp; ATP-grasp domain (PF02222; HMM-score: 64.5)
    GARS_A; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain (PF01071; HMM-score: 56.4)
    ATP-grasp_4; ATP-grasp domain (PF13535; HMM-score: 35.3)
    RimK; RimK-like ATP-grasp domain (PF08443; HMM-score: 30.3)
    ATP-grasp_5; ATP-grasp domain (PF13549; HMM-score: 30.2)
    ATP-grasp_2; ATP-grasp domain (PF08442; HMM-score: 23.7)
    no clan defined PrpR_N; Propionate catabolism activator (PF06506; HMM-score: 12.9)
    TORC_N; Transducer of regulated CREB activity, N terminus (PF12884; HMM-score: 12.5)

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

  • domains:
  • modifications:
  • cofactors: Mg2+, Mn2+
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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): 0.152665
    • TAT(Tat/SPI): 0.008979
    • LIPO(Sec/SPII): 0.022409
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MPKRNDIKTILVIGSGPIIIGQAAEFDYAGTQACLALKEEGYRVILVNSNPATIMTDKEIADKVYIEPLTHDFIARIIRKEQPDALLPTLGGQTGLNMAIQLHESGVLQDNNVQLLGTELTSIQQAEDREMFRTLMNDLNVPVPESDIVNTVEQAFKFKEQVGYPLIVRPAFTMGGTGGGICHNDEELHEIVSNGLHYSPATQCLLEKSIAGFKEIEYEVMRDKNDNAIVVCNMENIDPVGIHTGDSIVVAPSQTLSDVEYQMLRDVSLKVIRALGIEGGCNVQLALDPHSFDYYIIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEMLNPITGTSYAAFEPTLDYVISKIPRFPFDKFEKGERELGTQMKATGEVMAIGRTYEESLLKAIRSLEYGVHHLGLPNGESFDLDYIKERISHQDDERLFFIGEAIRRGTTLEEIHNMTQIDYFFLHKFQNIIDIEHQLKEHQGDLEYLKYAKDYGFSDKTIAHRFNMTEEEVYQLRMENDIKPVYKMVDTCAAEFESSTPYYYGTYETENESIVTDKEKILVLGSGPIRIGQGVEFDYATVHAVWAIQKAGYEAIIVNNNPETVSTDFSISDKLYFEPLTEEDVMNIINLEKPKGVVVQFGGQTAINLADKLAKHGVKILGTSLENLNRAEDRKEFEALLRKINVPQPQGKTATSPEEALANAAEIGYPVVVRPSYVLGGRAMEIVDNDKELENYMTQAVKASPEHPVLVDRYLTGKEIEVDAICDGETVIIPGIMEHIERAGVHSGDSIAVYPPQTLTEDELATLEDYTIKLAKGLNIIGLINIQFVIAHDGVYVLEVNPRSSRTVPFLSKITDIPMAQLAMRAIIGEKLTDMGYQEGVQPYAEGVFVKAPVFSFNKLKNVDITLGPEMKSTGEVMGKDTTLEKALFKGLTGSGVEVKDHGTVLMTVSDKDKEEVVKLAQRLNEVGYKILATSGTANKLAEYDIPAEVVGKIGGENDLLTRIQNGDVQIVINTMTKGKEVERDGFQIRRTTVENGIPCLTSLDTANALTNVIESMTFTMRQM

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 395 [5]
  • interaction partners:
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: pyrR leader (transcription antitermination) regulon
    pyrR leader(RNA)important in Pyrimidine metabolism; transcription unit transferred from N315 data RegPrecise binding of the PyrR antitermination protein

⊟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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 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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