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Protein

UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase

Gene

femX

Organism
Weissella viridescens (Lactobacillus viridescens)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism (PubMed:11083873, PubMed:4248527, PubMed:12679335, PubMed:15901708, PubMed:23744707). Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide (PubMed:15901708). Also acts on L-seryl-tRNA(Ser) (PubMed:4248527).5 Publications

Catalytic activityi

L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine.2 Publications

Kineticsi

  1. KM=15 µM for tRNA(Ala)1 Publication
  2. KM=1.7 µM for tRNA(Ala)1 Publication
  3. KM=42 µM for UDP-N-acetyl-muramoyl-pentapeptide1 Publication
  4. KM=79 µM for UDP-N-acetyl-muramoyl-pentapeptide1 Publication

    pH dependencei

    Optimum pH is 7.0-8.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041Substrate1 Publication
    Sitei109 – 1091Important for catalytic activity1 Publication
    Binding sitei212 – 2121Substrate1 Publication
    Binding sitei216 – 2161Substrate1 Publication
    Binding sitei257 – 2571Substrate1 Publication
    Sitei320 – 3201Important for catalytic activity1 Publication

    GO - Molecular functioni

    • UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15493.
    BRENDAi2.3.2.10. 2901.
    2.3.2.16. 2901.
    SABIO-RKQ9EY50.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase (EC:2.3.2.102 Publications)
    Gene namesi
    Name:femX1 Publication
    OrganismiWeissella viridescens (Lactobacillus viridescens)Imported
    Taxonomic identifieri1629 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeWeissella

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291Q → E: Loss of activity. 1 Publication
    Mutagenesisi29 – 291Q → T: Loss of activity. 1 Publication
    Mutagenesisi37 – 371K → M: Loss of activity. 2 Publications
    Mutagenesisi37 – 371K → R: Reduces activity 150-fold. 1 Publication
    Mutagenesisi37 – 371K → R: Reduces activity 200-fold. 1 Publication
    Mutagenesisi39 – 391N → L: No effect on activity. 1 Publication
    Mutagenesisi40 – 401W → F: Reduces activity 2-fold. 1 Publication
    Mutagenesisi71 – 711F → L: Reduces activity 2-fold. 1 Publication
    Mutagenesisi73 – 731Y → F: Reduces activity 2.5-fold. 1 Publication
    Mutagenesisi73 – 731Y → L: Reduces activity 2.5-fold. 1 Publication
    Mutagenesisi104 – 1041Y → F: No effect on activity. 1 Publication
    Mutagenesisi109 – 1091D → N: Reduces activity 200-fold. 1 Publication
    Mutagenesisi110 – 1101P → F: Loss of activity. 1 Publication
    Mutagenesisi110 – 1101P → H: Loss of activity. 1 Publication
    Mutagenesisi140 – 1401H → A: Reduces activity 5-fold. 1 Publication
    Mutagenesisi144 – 1441Q → E: Reduces activity 9-fold. 1 Publication
    Mutagenesisi144 – 1441Q → T: Sligthly reduces activity. 1 Publication
    Mutagenesisi196 – 1961F → L: Reduces activity 4-fold. 1 Publication
    Mutagenesisi196 – 1961F → Y: Sligthly reduces activity. 1 Publication
    Mutagenesisi205 – 2051E → Q: No effect on activity. 1 Publication
    Mutagenesisi207 – 2071H → A: Reduces activity 11-fold. 1 Publication
    Mutagenesisi209 – 2091I → A: Reduces activity 50-fold. 1 Publication
    Mutagenesisi210 – 2101T → A: Reduces activity 2-fold. 1 Publication
    Mutagenesisi212 – 2121R → K: Loss of activity. 1 Publication
    Mutagenesisi212 – 2121R → K: Loss of activity. 1 Publication
    Mutagenesisi212 – 2121R → M: Loss of activity. 2 Publications
    Mutagenesisi215 – 2151E → Q: No effect on activity. 1 Publication
    Mutagenesisi216 – 2161Y → F: Reduces activity 2.5-fold. 1 Publication
    Mutagenesisi216 – 2161Y → F: Reduces activity 20-fold. 1 Publication
    Mutagenesisi216 – 2161Y → F: Reduces activity 25-fold. 1 Publication
    Mutagenesisi216 – 2161Y → L: Loss of activity. 1 Publication
    Mutagenesisi257 – 2571Y → F: Reduces activity 2-fold. 1 Publication
    Mutagenesisi292 – 2921G → V: Loss of activity. 1 Publication
    Mutagenesisi305 – 3051F → A: Reduces activity 17-fold. 1 Publication
    Mutagenesisi305 – 3051F → L: Reduces activity 33-fold. 1 Publication
    Mutagenesisi305 – 3051F → L: Reduces activity 6-fold. 1 Publication
    Mutagenesisi305 – 3051F → Y: No effect on activity. 1 Publication
    Mutagenesisi306 – 3061K → A: Loss of activity. 1 Publication
    Mutagenesisi306 – 3061K → A: Reduces activity 12-fold. 1 Publication
    Mutagenesisi306 – 3061K → C: Reduces activity 2.5-fold. 1 Publication
    Mutagenesisi306 – 3061K → M: Reduces activity 200-fold. 1 Publication
    Mutagenesisi306 – 3061K → N: Reduces activity 11-fold. 1 Publication
    Mutagenesisi306 – 3061K → R: Loss of activity. 1 Publication
    Mutagenesisi316 – 3161E → Q: Reduces activity 3-fold. 1 Publication
    Mutagenesisi319 – 3191G → S: Reduces activity 8-fold. 1 Publication
    Mutagenesisi319 – 3191G → V: Reduces activity 20-fold. 1 Publication
    Mutagenesisi320 – 3201E → Q: Reduces activity 25-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 336335UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferasePRO_0000430779Add
    BLAST

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2113Combined sources
    Helixi27 – 293Combined sources
    Helixi31 – 366Combined sources
    Turni37 – 393Combined sources
    Beta strandi40 – 489Combined sources
    Beta strandi54 – 6310Combined sources
    Beta strandi66 – 749Combined sources
    Helixi85 – 9915Combined sources
    Beta strandi103 – 1086Combined sources
    Helixi116 – 1249Combined sources
    Beta strandi128 – 1314Combined sources
    Helixi132 – 1343Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi139 – 1413Combined sources
    Beta strandi142 – 1443Combined sources
    Beta strandi146 – 1527Combined sources
    Helixi153 – 1553Combined sources
    Helixi162 – 1654Combined sources
    Helixi168 – 17912Combined sources
    Beta strandi182 – 1876Combined sources
    Helixi190 – 20718Combined sources
    Helixi214 – 22310Combined sources
    Turni226 – 2283Combined sources
    Beta strandi229 – 2368Combined sources
    Beta strandi239 – 24911Combined sources
    Beta strandi252 – 2609Combined sources
    Helixi268 – 28215Combined sources
    Beta strandi286 – 2927Combined sources
    Helixi301 – 3099Combined sources
    Beta strandi315 – 3173Combined sources
    Beta strandi320 – 3256Combined sources
    Helixi327 – 3337Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NE9X-ray1.70A2-336[»]
    1P4NX-ray1.90A2-336[»]
    1XE4X-ray1.95A2-336[»]
    1XF8X-ray1.90A2-336[»]
    1XIXX-ray2.00A2-336[»]
    3GKRX-ray1.60A1-336[»]
    4II9X-ray1.66A1-336[»]
    ProteinModelPortaliQ9EY50.
    SMRiQ9EY50. Positions 2-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9EY50.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 404Substrate binding1 Publication

    Sequence similaritiesi

    Belongs to the FemABX family.Curated

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR003447. FEMABX.
    [Graphical view]
    PfamiPF02388. FemAB. 2 hits.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 2 hits.
    PROSITEiPS51191. FEMABX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9EY50-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPVLNLNDPQ AVERYEEFMR QSPYGQVTQD LGWAKVKNNW EPVDVYLEDD
    60 70 80 90 100
    QGAIIAAMSM LLGDTPTDKK FAYASKGPVM DVTDVDLLDR LVDEAVKALD
    110 120 130 140 150
    GRAYVLRFDP EVAYSDEFNT TLQDHGYVTR NRNVADAGMH ATIQPRLNMV
    160 170 180 190 200
    LDLTKFPDAK TTLDLYPSKT KSKIKRPFRD GVEVHSGNSA TELDEFFKTY
    210 220 230 240 250
    TTMAERHGIT HRPIEYFQRM QAAFDADTMR IFVAEREGKL LSTGIALKYG
    260 270 280 290 300
    RKIWYMYAGS MDGNTYYAPY AVQSEMIQWA LDTNTDLYDL GGIESESTDD
    310 320 330
    SLYVFKHVFV KDAPREYIGE IDKVLDPEVY AELVKD
    Length:336
    Mass (Da):38,284
    Last modified:March 1, 2001 - v1
    Checksum:iAFB94A2718148C3C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY008262 Genomic DNA. Translation: AAG21689.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY008262 Genomic DNA. Translation: AAG21689.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NE9X-ray1.70A2-336[»]
    1P4NX-ray1.90A2-336[»]
    1XE4X-ray1.95A2-336[»]
    1XF8X-ray1.90A2-336[»]
    1XIXX-ray2.00A2-336[»]
    3GKRX-ray1.60A1-336[»]
    4II9X-ray1.66A1-336[»]
    ProteinModelPortaliQ9EY50.
    SMRiQ9EY50. Positions 2-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15493.
    BRENDAi2.3.2.10. 2901.
    2.3.2.16. 2901.
    SABIO-RKQ9EY50.

    Miscellaneous databases

    EvolutionaryTraceiQ9EY50.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR003447. FEMABX.
    [Graphical view]
    PfamiPF02388. FemAB. 2 hits.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 2 hits.
    PROSITEiPS51191. FEMABX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets."
      Hegde S.S., Shrader T.E.
      J. Biol. Chem. 276:6998-7003(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24; 161-169 AND 316-333, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-29; TYR-73; PRO-110; GLN-144; PHE-196; TYR-216; GLY-292; PHE-305; LYS-306 AND GLY-319.
    2. "Biosynthesis of the peptidoglycan of bacterial cell walls. 18. Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens."
      Plapp R., Strominger J.L.
      J. Biol. Chem. 245:3675-3682(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    3. "Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase)."
      Hegde S.S., Blanchard J.S.
      J. Biol. Chem. 278:22861-22867(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-109; GLU-205; GLU-215; GLU-316 AND GLU-320.
    4. "Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition."
      Biarrotte-Sorin S., Maillard A.P., Delettre J., Sougakoff W., Arthur M., Mayer C.
      Structure 12:257-267(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-336 IN COMPLEX WITH SUBSTRATE.
    5. "Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens."
      Maillard A.P., Biarrotte-Sorin S., Villet R., Mesnage S., Bouhss A., Sougakoff W., Mayer C., Arthur M.
      J. Bacteriol. 187:3833-3838(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-336, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-37; ARG-212 AND TYR-216.
    6. "Structure of Weissella viridescens FemX with the UDP-MurNAc-hexapeptide product of the alanine transfer reaction."
      Delfosse V., Piton J., Villet R., Lecerf M., Arthur M., Mayer C.
      Submitted (MAR-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
    7. "The structure of FemX(Wv) in complex with a peptidyl-RNA conjugate: mechanism of aminoacyl transfer from Ala-tRNA(Ala) to peptidoglycan precursors."
      Fonvielle M., Li de La Sierra-Gallay I., El-Sagheer A.H., Lecerf M., Patin D., Mellal D., Mayer C., Blanot D., Gale N., Brown T., van Tilbeurgh H., Etheve-Quelquejeu M., Arthur M.
      Angew. Chem. Int. Ed. 52:7278-7281(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS), FUNCTION, MUTAGENESIS OF LYS-37; ASN-39; TRP-40; PHE-71; TYR-104; HIS-140; HIS-207; ILE-209; THR-210; ARG-212; TYR-216; TYR-257; PHE-305 AND LYS-306.

    Entry informationi

    Entry nameiFEMX_WEIVI
    AccessioniPrimary (citable) accession number: Q9EY50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: March 1, 2001
    Last modified: May 27, 2015
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.