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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02561
- 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: SAOUHSC_02561
- symbol: ureC
- product: urease subunit alpha
- replicon: chromosome
- strand: +
- coordinates: 2352985..2354700
- length: 1716
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921558 NCBI
- RefSeq: YP_501022 NCBI
- BioCyc: G1I0R-2418 BioCyc
- MicrobesOnline: 1290993 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1681ATGAGCTTTAAAATGACGCAAAATCAATATACGAGCTTATACGGTCCAACTGTTGGAGAT
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
GAGTTACCATTAACTCAAAGATACTTCTTATTCTAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_02561
- 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? ExPASyUrease Urea + H2O = CO2 + 2 NH3
- TIGRFAM: Central intermediary metabolism Nitrogen metabolism urease, alpha subunit (TIGR01792; EC 3.5.1.5; HMM-score: 1027.6)and 8 morePurines, 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)Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis dihydroorotase, multifunctional complex type (TIGR00857; EC 3.5.2.3; HMM-score: 24.3)Energy metabolism Amino acids and amines imidazolonepropionase (TIGR01224; EC 3.5.2.7; HMM-score: 22.9)Purines, pyrimidines, nucleosides, and nucleotides Other guanine deaminase (TIGR02967; EC 3.5.4.3; HMM-score: 18)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 - PFAM: Amidohydrolase (CL0034) Amidohydro_1; Amidohydrolase family (PF01979; HMM-score: 258.7)and 2 moreUrease_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 [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01170 (carB) carbamoyl phosphate synthase large subunit [3] (data from MRSA252) SAOUHSC_01778 (clpX) ATP-dependent protease ATP-binding subunit ClpX [3] (data from MRSA252) SAOUHSC_02318 (ddl) D-alanyl-alanine synthetase A [3] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_02116 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [3] (data from MRSA252) SAOUHSC_01276 (glpK) glycerol kinase [3] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SAOUHSC_00493 (lysS) lysyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00743 (nrdF) ribonucleotide-diphosphate reductase subunit beta [3] (data from MRSA252) SAOUHSC_01235 (pyrH) uridylate kinase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_02353 (upp) uracil phosphoribosyltransferase [3] (data from MRSA252) SAOUHSC_00002 DNA polymerase III subunit beta [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00346 GTP-dependent nucleic acid-binding protein EngD [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00742 ribonucleotide-diphosphate reductase subunit alpha [3] (data from MRSA252) SAOUHSC_00847 ABC transporter ATP-binding protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01007 bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01240 prolyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01451 threonine dehydratase [3] (data from MRSA252) SAOUHSC_01623 acetyl-CoA carboxylase biotin carboxylase subunit [3] (data from MRSA252) SAOUHSC_01633 glycine dehydrogenase subunit 1 [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01909 S-adenosylmethionine synthetase [3] (data from MRSA252) SAOUHSC_02337 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02363 aldehyde dehydrogenase [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02512a 30S ribosomal protein S10 [3] (data from MRSA252) SAOUHSC_02574 hypothetical protein [3] (data from MRSA252) SAOUHSC_02793 hypothetical protein [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: ureA > ureB > ureC > ureE > SAOUHSC_02563 > SAOUHSC_02564 > SAOUHSC_02565
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟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]
- ↑ 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) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 3.62 3.63 3.64 3.65 3.66 3.67 3.68 3.69 3.70 3.71 3.72 3.73 3.74 3.75 3.76 3.77 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) - ↑ 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)