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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2253 [new locus tag: SACOL_RS11845 ]
  • pan locus tag?: SAUPAN005718000
  • symbol: femX
  • pan gene symbol?: femX
  • synonym:
  • product: femX protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2253 [new locus tag: SACOL_RS11845 ]
  • symbol: femX
  • product: femX protein
  • replicon: chromosome
  • strand: -
  • coordinates: 2319781..2321046
  • length: 1266
  • 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
    ATGGAAAAGATGCATATCACTAATCAGGAACATGACGCATTTGTTAAATCCCACCCAAAT
    GGAGATTTATTACAATTAACGAAATGGGCAGAAACAAAGAAATTAACTGGATGGTACGCG
    CGAAGAATCGCTGTAGGTCGTGACGGTGAAGTTCAGGGTGTTGCGCAGTTACTTTTTAAA
    AAAGTACCTAAATTACCTTATACGCTATGTTATATTTCGCGTGGTTTTGTTGTTGATTAT
    AGTAATAAAGAAGCGTTAAATGCATTGTTAGACAGTGCAAAAGAAATTGCTAAAGCTGAG
    AAAACGTATGCAATTAAAATCGATCCTGATGTTGAAGTTGATAAAGGTACAGATGCTTTG
    CAAAATTTGAAAGCGCTTGGTTTTAAACATAAAGGATTTAAAGAAGGTTTATCAAAAGAC
    TACATCCAACCACGTATGACTATGATTACACCAATTGATAAAAATGATGATGAGTTATTA
    AATAGTTTTGAACGCCGAAATCGTTCAAAAGTGCGCTTGGCTTTAAAGCGAGGTACGACA
    GTAGAACGATCTGATAGAGAAGGTTTAAAAACATTTGCTGAGTTAATGAAAATCACTGGG
    GAACGCGATGGCTTCTTAACGCGTGATATTAGTTACTTTGAAAATATTTATGATGCGTTG
    CATGAAGATGGAGATGCTGAACTATTTTTAGTAAAGTTGGATCCAAAAGAAAATATAGCG
    AAAGTAAATCAAGAATTGAATGAACTTCATGCCGAAATTGCTAAATGGCAGCAGAAGATG
    AAAACATCTGAAAAGCAAGCTAAAAAAGCGCAAAATATGATTAATGATGCGCAAAATAAA
    ATTGCTAAAAATGAAGATTTAAAACGAGACCTAGAAGCTTTAGAAAAGGAACATCCTGAA
    GGTATTTATCTTTCTGGTGCACTATTAATGTTTGCTGGCTCAAAATCATATTACTTATAT
    GGTGCGTCTTCTAATGAATTTAGAGATTTTTTACCAAATCATCATATGCAGTATACGATG
    ATGAAGTATGCACGTGAACATGGTGCAACAACTTACGATTTCGGTGGTACAGATAATGAT
    CCAGATAAAGACTCAGAACATTATGGATTATGGGCATTTAAAAAAGTGTGGGGAACATAC
    TTAAGTGAAAAGATTGGTGAATTTGATTATGTATTGAATCAGCCATTGTACCAATTAATT
    GAGCAAGTTAAACCGCGTTTAACAAAAGCTAAAATTAAAATATCTCGTAAATTAAAACGA
    AAATAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1266

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2253 [new locus tag: SACOL_RS11845 ]
  • symbol: FemX
  • description: femX protein
  • length: 421
  • theoretical pI: 9.31875
  • theoretical MW: 48551.1
  • GRAVY: -0.728741

⊟Function[edit | edit source]

  • reaction:
    EC 2.3.2.16?  ExPASy
    Lipid II:glycine glycyltransferase MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNA(Gly) = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNA(Gly)
  • TIGRFAM:
    Unknown function General FemAB-related protein, PEP-CTERM system-associated (TIGR03019; HMM-score: 57.1)
    and 4 more
    SH3 domain protein (TIGR04211; HMM-score: 17.6)
    two transmembrane protein (TIGR04527; HMM-score: 9.7)
    CRISPR type III-A/MTUBE-associated protein Csm2 (TIGR01870; HMM-score: 8.1)
    phage lysis regulatory protein, LysB family (TIGR03495; HMM-score: 5.9)
  • TheSEED  :
    • tRNA-dependent lipid II--glycine ligase (FmhB)
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory tRNA-dependent amino acid transfers  tRNA-dependent lipid II--glycine ligase (FmhB)
  • PFAM:
    Acetyltrans (CL0257) FemAB; FemAB family (PF02388; HMM-score: 277.6)
    and 25 more
    Acetyltransf_6; Acetyltransferase (GNAT) domain (PF13480; HMM-score: 50.1)
    P-loop_NTPase (CL0023) AAA_13; AAA domain (PF13166; HMM-score: 17.6)
    no clan defined Spc7; Spc7 kinetochore protein (PF08317; HMM-score: 17.4)
    Laminin_II; Laminin Domain II (PF06009; HMM-score: 16.8)
    MIS13; Mis12-Mtw1 protein family (PF08202; HMM-score: 16.3)
    FapA; Flagellar Assembly Protein A (PF03961; HMM-score: 16)
    PDDEXK (CL0236) RmuC; RmuC family (PF02646; HMM-score: 15.4)
    no clan defined IncA; IncA protein (PF04156; HMM-score: 15.4)
    Tropomyosin-lke (CL0452) Tropomyosin_1; Tropomyosin like (PF12718; HMM-score: 13.9)
    no clan defined Cep57_CLD_2; Centrosome localisation domain of PPC89 (PF14197; HMM-score: 13.3)
    TMPIT; TMPIT-like protein (PF07851; HMM-score: 13.2)
    ExbD; Biopolymer transport protein ExbD/TolR (PF02472; HMM-score: 12.4)
    FtsL (CL0225) DivIC; Septum formation initiator (PF04977; HMM-score: 12.1)
    no clan defined TMF_TATA_bd; TATA element modulatory factor 1 TATA binding (PF12325; HMM-score: 12.1)
    TRAF_BIRC3_bd; TNF receptor-associated factor BIRC3 binding domain (PF16673; HMM-score: 12.1)
    DUF5069; Domain of unknown function (DUF5069) (PF16798; HMM-score: 12)
    DUF3987; Protein of unknown function (DUF3987) (PF13148; HMM-score: 11.1)
    BRE1; BRE1 E3 ubiquitin ligase (PF08647; HMM-score: 10.8)
    HTH (CL0123) Mnd1; Mnd1 family (PF03962; HMM-score: 10.6)
    no clan defined ISG65-75; Invariant surface glycoprotein (PF11727; HMM-score: 10.2)
    Ax_dynein_light; Axonemal dynein light chain (PF10211; HMM-score: 9.6)
    PCRF; PCRF domain (PF03462; HMM-score: 9)
    XhlA; Haemolysin XhlA (PF10779; HMM-score: 8.6)
    DUF724; Protein of unknown function (DUF724) (PF05266; HMM-score: 8.3)
    OmpH; Outer membrane protein (OmpH-like) (PF03938; HMM-score: 7.1)

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

  • domains:
  • modifications:
  • cofactors:
  • 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): 0.007329
    • TAT(Tat/SPI): 0.000932
    • LIPO(Sec/SPII): 0.000722
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MEKMHITNQEHDAFVKSHPNGDLLQLTKWAETKKLTGWYARRIAVGRDGEVQGVAQLLFKKVPKLPYTLCYISRGFVVDYSNKEALNALLDSAKEIAKAEKTYAIKIDPDVEVDKGTDALQNLKALGFKHKGFKEGLSKDYIQPRMTMITPIDKNDDELLNSFERRNRSKVRLALKRGTTVERSDREGLKTFAELMKITGERDGFLTRDISYFENIYDALHEDGDAELFLVKLDPKENIAKVNQELNELHAEIAKWQQKMKTSEKQAKKAQNMINDAQNKIAKNEDLKRDLEALEKEHPEGIYLSGALLMFAGSKSYYLYGASSNEFRDFLPNHHMQYTMMKYAREHGATTYDFGGTDNDPDKDSEHYGLWAFKKVWGTYLSEKIGEFDYVLNQPLYQLIEQVKPRLTKAKIKISRKLKRK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 497 [4]
  • interaction partners:
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [5] (data from MRSA252)
    SACOL1536(rluB)ribosomal large subunit pseudouridine synthase B  [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)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2229(rplN)50S ribosomal protein L14  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [5] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL2228(rplX)50S ribosomal protein L24  [5] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [5] (data from MRSA252)
    SACOL2231(rpmC)50S ribosomal protein L29  [5] (data from MRSA252)
    SACOL1726(rpmI)50S ribosomal protein L35  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [5] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL0439(rpsR)30S ribosomal protein S18  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL03035'-nucleotidase  [5] (data from MRSA252)
    SACOL0578RNA methyltransferase  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0742hypothetical protein  [5] (data from MRSA252)
    SACOL1098hypothetical protein  [5] (data from MRSA252)
    SACOL1426hypothetical protein  [5] (data from MRSA252)
    SACOL1615DEAD/DEAH box helicase  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL2072DEAD/DEAH box helicase  [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: 16.44 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 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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