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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)DescriptionActionsGraphical viewLength
    Binding sitei104Substrate1 Publication1
    Sitei109Important for catalytic activity1 Publication1
    Binding sitei212Substrate1 Publication1
    Binding sitei216Substrate1 Publication1
    Binding sitei257Substrate1 Publication1
    Sitei320Important for catalytic activity1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi29Q → E: Loss of activity. 1 Publication1
    Mutagenesisi29Q → T: Loss of activity. 1 Publication1
    Mutagenesisi37K → M: Loss of activity. 2 Publications1
    Mutagenesisi37K → R: Reduces activity 150-fold. 1 Publication1
    Mutagenesisi37K → R: Reduces activity 200-fold. 1 Publication1
    Mutagenesisi39N → L: No effect on activity. 1 Publication1
    Mutagenesisi40W → F: Reduces activity 2-fold. 1 Publication1
    Mutagenesisi71F → L: Reduces activity 2-fold. 1 Publication1
    Mutagenesisi73Y → F: Reduces activity 2.5-fold. 1 Publication1
    Mutagenesisi73Y → L: Reduces activity 2.5-fold. 1 Publication1
    Mutagenesisi104Y → F: No effect on activity. 1 Publication1
    Mutagenesisi109D → N: Reduces activity 200-fold. 1 Publication1
    Mutagenesisi110P → F: Loss of activity. 1 Publication1
    Mutagenesisi110P → H: Loss of activity. 1 Publication1
    Mutagenesisi140H → A: Reduces activity 5-fold. 1 Publication1
    Mutagenesisi144Q → E: Reduces activity 9-fold. 1 Publication1
    Mutagenesisi144Q → T: Sligthly reduces activity. 1 Publication1
    Mutagenesisi196F → L: Reduces activity 4-fold. 1 Publication1
    Mutagenesisi196F → Y: Sligthly reduces activity. 1 Publication1
    Mutagenesisi205E → Q: No effect on activity. 1 Publication1
    Mutagenesisi207H → A: Reduces activity 11-fold. 1 Publication1
    Mutagenesisi209I → A: Reduces activity 50-fold. 1 Publication1
    Mutagenesisi210T → A: Reduces activity 2-fold. 1 Publication1
    Mutagenesisi212R → K: Loss of activity. 1 Publication1
    Mutagenesisi212R → M: Loss of activity. 2 Publications1
    Mutagenesisi215E → Q: No effect on activity. 1 Publication1
    Mutagenesisi216Y → F: Reduced activity. 2 Publications1
    Mutagenesisi216Y → F: Reduces activity 25-fold. 1 Publication1
    Mutagenesisi216Y → L: Loss of activity. 1 Publication1
    Mutagenesisi257Y → F: Reduces activity 2-fold. 1 Publication1
    Mutagenesisi292G → V: Loss of activity. 1 Publication1
    Mutagenesisi305F → A: Reduces activity 17-fold. 1 Publication1
    Mutagenesisi305F → L: Reduces activity 33-fold. 1 Publication1
    Mutagenesisi305F → L: Reduces activity 6-fold. 1 Publication1
    Mutagenesisi305F → Y: No effect on activity. 1 Publication1
    Mutagenesisi306K → A: Loss of activity. 1 Publication1
    Mutagenesisi306K → A: Reduces activity 12-fold. 1 Publication1
    Mutagenesisi306K → C: Reduces activity 2.5-fold. 1 Publication1
    Mutagenesisi306K → M: Reduces activity 200-fold. 1 Publication1
    Mutagenesisi306K → N: Reduces activity 11-fold. 1 Publication1
    Mutagenesisi306K → R: Loss of activity. 1 Publication1
    Mutagenesisi316E → Q: Reduces activity 3-fold. 1 Publication1
    Mutagenesisi319G → S: Reduces activity 8-fold. 1 Publication1
    Mutagenesisi319G → V: Reduces activity 20-fold. 1 Publication1
    Mutagenesisi320E → Q: Reduces activity 25-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004307792 – 336UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferaseAdd BLAST335

    Structurei

    Secondary structure

    1336
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 21Combined sources13
    Helixi27 – 29Combined sources3
    Helixi31 – 36Combined sources6
    Turni37 – 39Combined sources3
    Beta strandi40 – 48Combined sources9
    Beta strandi54 – 63Combined sources10
    Beta strandi66 – 74Combined sources9
    Helixi85 – 99Combined sources15
    Beta strandi103 – 108Combined sources6
    Helixi116 – 124Combined sources9
    Beta strandi128 – 131Combined sources4
    Helixi132 – 134Combined sources3
    Beta strandi136 – 138Combined sources3
    Helixi139 – 141Combined sources3
    Beta strandi142 – 144Combined sources3
    Beta strandi146 – 152Combined sources7
    Helixi153 – 155Combined sources3
    Helixi162 – 165Combined sources4
    Helixi168 – 179Combined sources12
    Beta strandi182 – 187Combined sources6
    Helixi190 – 207Combined sources18
    Helixi214 – 223Combined sources10
    Turni226 – 228Combined sources3
    Beta strandi229 – 236Combined sources8
    Beta strandi239 – 249Combined sources11
    Beta strandi252 – 260Combined sources9
    Helixi268 – 282Combined sources15
    Beta strandi286 – 292Combined sources7
    Helixi301 – 309Combined sources9
    Beta strandi315 – 317Combined sources3
    Beta strandi320 – 325Combined sources6
    Helixi327 – 333Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9EY50.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni37 – 40Substrate binding1 Publication4

    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.
    RefSeqiWP_057745451.1. NZ_JQBM01000002.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY008262 Genomic DNA. Translation: AAG21689.1.
    RefSeqiWP_057745451.1. NZ_JQBM01000002.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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...

    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: November 2, 2016
    This is version 65 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

    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 one 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.