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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

  1. UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan biosynthetic process Source: UniProtKB
  3. regulation of cell shape Source: UniProtKB-KW
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.
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.
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: February 4, 2015
This is version 56 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.