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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2282 [new locus tag: SACOL_RS11995 ]
  • pan locus tag?: SAUPAN005755000
  • symbol: ureC
  • pan gene symbol?: ureC
  • synonym:
  • product: urease subunit alpha

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2282 [new locus tag: SACOL_RS11995 ]
  • symbol: ureC
  • product: urease subunit alpha
  • replicon: chromosome
  • strand: +
  • coordinates: 2342319..2344034
  • length: 1716
  • 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
    ATGAGCTTTAAAATGACGCAAAATCAATATACGAGCTTATACGGTCCAACTGTTGGAGAT
    TCCATTCGTTTAGGTGATACGAATCTATTTGCTCAAATAGAAAAAGACTATGCGGTTTAT
    GGTGAAGAAGCTACTTTTGGTGGTGGTAAATCTATTAGAGACGGTATGGCGCAAAATCCT
    CGTGTAACACGTGATGACGTGAACGTTGCAGACCTTGTCATTTCTAATGCCGTTATTATC
    GATTACGATAAAGTGGTTAAAGCTGATATAGGCATTAAAAATGGTTATATTTTCGCCATA
    GGTAATGCCGGCAACCCAGATATAATGGATAATGTCGACATTATTATAGGTTCAACAACA
    GATATCATTGCCGCTGAAGGTAAAATCGTCACTGCTGGTGGTATTGATACTCATGTTCAT
    TTTATTAATCCTGAACAAGCAGAGGTCGCATTAGAAAGTGGTATTACGACTCATATTGGT
    GGTGGTACTGGTGCTTCAGAAGGTTCTAAAGCAACAACTGTAACTCCAGGTCCATGGCAT
    ATTCATAGAATGTTAGAAGCTGCCGAAGGTTTACCGATTAATGTCGGTTTTACAGGTAAA
    GGACAAGCAACAAATCCAACTGCACTCATTGAACAAATCAATGCCGGAGCAATTGGATTA
    AAAGTACATGAAGACTGGGGTGCAACACCATCTGCTTTGAGTCATGCATTAGATGTTGCT
    GATGAATTTGATGTTCAAATTGCATTACATGCAGATACTTTAAATGAAGCAGGATTTATG
    GAAGACACAATGGCTGCTGTTAAAGACCGTGTACTTCATATGTACCATACTGAAGGTGCT
    GGTGGCGGTCATGCGCCTGATTTAATTAAATCCGCTGCATTTTCAAATATTTTACCTTCA
    TCTACAAATCCAACTTTGCCTTATACACATAATACTGTAGATGAACATTTAGATATGGTA
    ATGATTACTCACCATTTAAATGCGGCTATTCCTGAAGATATCGCATTCGCAGATTCACGT
    ATTCGTAAAGAAACGATTGCAGCAGAAGATGTTCTGCAAGATATGGGTGTATTCAGTATG
    ATTAGTTCCGATTCACAAGCAATGGGCCGTGTAGGTGAAGTAATTACACGAACATGGCAA
    GTAGCACATCGCATGAAAGAACAACGTGGTCCTTTAGATGGTGATTTTGAACATAATGAT
    AATAATCGCATCAAACGTTATATCGCTAAATATACAATTAACCCAGCAATTACACATGGT
    ATTTCTGAATATGTAGGATCTATCGAGCCGGGCAAACTAGCTGACATTGTCTTATGGGAC
    CCAATTTTCTTTGGGGTTAAACCTGAATTAGTTGTAAAGGGCGGATTAATTAACTCTGCC
    GTAAATGGCGATGCAAATGGTTCTATACCTACATCTGAACCGATGAAGTACCGTAAAATG
    TATGGTCAATACGGCGGAAACCTTACAAGTACGTCAATGACATTCGTGTCTAAAACTGCT
    TATGAAAATGGTATCAATCGTGCATTAAATTTAAAACGCATGGTGCGTCCAGTTAAAAAT
    ATTAGACAATTATCTAAAGCAGATATGAAAAATAACAGTGCAACACCTAAATTAGACGTT
    GATCCACAAACATATGAAGTATATGTAGATGGAGAAAAAATTACAAGTAATGCAGCAACT
    GAGTTACCATTAACTCAAAGATACTTCTTATTCTAG
    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
    1716

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2282 [new locus tag: SACOL_RS11995 ]
  • symbol: UreC
  • description: urease subunit alpha
  • length: 571
  • theoretical pI: 5.06399
  • theoretical MW: 61779.2
  • GRAVY: -0.226445

⊟Function[edit | edit source]

  • reaction:
    EC 3.5.1.5?  ExPASy
    Urease Urea + H2O = CO2 + 2 NH3
  • TIGRFAM:
    Metabolism Central intermediary metabolism Nitrogen metabolism urease, alpha subunit (TIGR01792; EC 3.5.1.5; HMM-score: 1027.6)
    and 8 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides adenine deaminase (TIGR01178; EC 3.5.4.2; HMM-score: 28)
    allantoinase (TIGR03178; EC 3.5.2.5; HMM-score: 27.9)
    dihydropyrimidinase (TIGR02033; EC 3.5.2.2; HMM-score: 25.4)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis dihydroorotase, multifunctional complex type (TIGR00857; EC 3.5.2.3; HMM-score: 24.3)
    Metabolism Energy metabolism Amino acids and amines imidazolonepropionase (TIGR01224; EC 3.5.2.7; HMM-score: 22.9)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Other guanine deaminase (TIGR02967; EC 3.5.4.3; HMM-score: 18)
    Metabolism Energy metabolism Other phosphonate metabolism protein PhnM (TIGR02318; HMM-score: 16.3)
    formylmethanofuran dehydrogenase subunit A (TIGR03121; EC 1.2.99.5; HMM-score: 13)
  • TheSEED  :
    • Urease alpha subunit (EC 3.5.1.5)
    Amino Acids and Derivatives Arginine; urea cycle, polyamines Urea decomposition  Urease alpha subunit (EC 3.5.1.5)
    and 1 more
    Amino Acids and Derivatives Arginine; urea cycle, polyamines Urease subunits  Urease alpha subunit (EC 3.5.1.5)
  • PFAM:
    Amidohydrolase (CL0034) Amidohydro_1; Amidohydrolase family (PF01979; HMM-score: 258.7)
    and 2 more
    Urease_alpha; Urease alpha-subunit, N-terminal domain (PF00449; HMM-score: 168.9)
    Amidohydro_3; Amidohydrolase family (PF07969; HMM-score: 44.3)

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

  • domains:
  • modifications:
  • cofactors: Ni cation
  • 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): 0.011924
    • TAT(Tat/SPI): 0.00069
    • LIPO(Sec/SPII): 0.002167
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSFKMTQNQYTSLYGPTVGDSIRLGDTNLFAQIEKDYAVYGEEATFGGGKSIRDGMAQNPRVTRDDVNVADLVISNAVIIDYDKVVKADIGIKNGYIFAIGNAGNPDIMDNVDIIIGSTTDIIAAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGGGTGASEGSKATTVTPGPWHIHRMLEAAEGLPINVGFTGKGQATNPTALIEQINAGAIGLKVHEDWGATPSALSHALDVADEFDVQIALHADTLNEAGFMEDTMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAFSNILPSSTNPTLPYTHNTVDEHLDMVMITHHLNAAIPEDIAFADSRIRKETIAAEDVLQDMGVFSMISSDSQAMGRVGEVITRTWQVAHRMKEQRGPLDGDFEHNDNNRIKRYIAKYTINPAITHGISEYVGSIEPGKLADIVLWDPIFFGVKPELVVKGGLINSAVNGDANGSIPTSEPMKYRKMYGQYGGNLTSTSMTFVSKTAYENGINRALNLKRMVRPVKNIRQLSKADMKNNSATPKLDVDPQTYEVYVDGEKITSNAATELPLTQRYFLF

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2]
  • quantitative data / protein copy number per cell: 208 [3]
  • interaction partners:
    SACOL1571(accC)acetyl-CoA carboxylase biotin carboxylase subunit  [4] (data from MRSA252)
    SACOL1760(ackA)acetate kinase  [4] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [4] (data from MRSA252)
    SACOL1215(carB)carbamoyl phosphate synthase large subunit  [4] (data from MRSA252)
    SACOL1721(clpX)ATP-dependent protease ATP-binding subunit ClpX  [4] (data from MRSA252)
    SACOL2074(ddl)D-alanyl-alanine synthetase A  [4] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [4] (data from MRSA252)
    SACOL0002(dnaN)DNA polymerase III subunit beta  [4] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [4] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [4] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [4] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [4] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [4] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [4] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [4] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [4] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [4] (data from MRSA252)
    SACOL1320(glpK)glycerol kinase  [4] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [4] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [4] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [4] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [4] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [4] (data from MRSA252)
    SACOL0562(lysS)lysyl-tRNA synthetase  [4] (data from MRSA252)
    SACOL1837(metK)S-adenosylmethionine synthetase  [4] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [4] (data from MRSA252)
    SACOL2092(murAA)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [4] (data from MRSA252)
    SACOL2116(murAB)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [4] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [4] (data from MRSA252)
    SACOL0793(nrdF)ribonucleotide-diphosphate reductase subunit beta  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [4] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [4] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [4] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [4] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [4] (data from MRSA252)
    SACOL1282(proS)prolyl-tRNA synthetase  [4] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [4] (data from MRSA252)
    SACOL1277(pyrH)uridylate kinase  [4] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [4] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [4] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [4] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [4] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [4] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [4] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [4] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [4] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [4] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [4] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [4] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [4] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [4] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [4] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [4] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [4] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [4] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [4] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [4] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [4] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [4] (data from MRSA252)
    SACOL0435GTP-dependent nucleic acid-binding protein EngD  [4] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [4] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [4] (data from MRSA252)
    SACOL0914FeS assembly ATPase SufC  [4] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [4] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [4] (data from MRSA252)
    SACOL1594glycine dehydrogenase subunit 1  [4] (data from MRSA252)
    SACOL1759universal stress protein  [4] (data from MRSA252)
    SACOL2114aldehyde dehydrogenase  [4] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [4] (data from MRSA252)
    SACOL2293NAD/NADP octopine/nopaline dehydrogenase  [4] (data from MRSA252)
    SACOL2501phosphoglucomutase/phosphomannomutase  [4] (data from MRSA252)
    SACOL2553pyruvate oxidase  [4] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [4] (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: 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. ↑ 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)
  3. ↑ 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)
  4. ↑ 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 4.49 4.50 4.51 4.52 4.53 4.54 4.55 4.56 4.57 4.58 4.59 4.60 4.61 4.62 4.63 4.64 4.65 4.66 4.67 4.68 4.69 4.70 4.71 4.72 4.73 4.74 4.75 4.76 4.77 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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