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P0A0A5 (FEMA_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminoacyltransferase FemA

EC=2.3.2.17
Alternative name(s):
Factor essential for expression of methicillin resistance A
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Gene names
Name:femA
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. Adds glycines 2 and 3 of the pentaglycine bridge, using glycyl-tRNA(Gly) as donor.

Catalytic activity

MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNA = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNA.

Subunit structure

Homodimer. Interacts with FemB By similarity.

Subcellular location

Cytoplasm Ref.2.

Miscellaneous

Since cross-linking between the peptide strands is critical for maintaining stability of the cell wall, FemA is a potential target for the development of new antibacterial agents.

Sequence similarities

Belongs to the FemABX family.

Sequence caution

The sequence CAA35679.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Aminoacyltransferase FemA
PRO_0000204735

Secondary structure

.............................................................. 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A0A5 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: E6790BD7C8B50297

FASTA42049,124
        10         20         30         40         50         60 
MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA 

        70         80         90        100        110        120 
VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG 

       130        140        150        160        170        180 
EITGNAGNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK 

       190        200        210        220        230        240 
RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL 

       250        260        270        280        290        300 
AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG 

       310        320        330        340        350        360 
KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR 

       370        380        390        400        410        420 
YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF 

« Hide

References

[1]"FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization."
Berger-Baechi B., Barberis-Maino L., Straessle A., Kayser F.H.
Mol. Gen. Genet. 219:263-269(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"FemA of Staphylococcus aureus: isolation and immunodetection."
Johnson S., Krueger D., Labischinski H.
FEMS Microbiol. Lett. 132:221-228(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: SG511.
[3]"X-ray crystal structure of Staphylococcus aureus FemA."
Benson T.E., Prince D.B., Mutchler V.T., Curry K.A., Ho A.M., Sarver R.W., Hagadorn J.C., Choi G.H., Garlick R.L.
Structure 10:1107-1115(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17688 Genomic DNA. Translation: CAA35679.1. Different initiation.
PIRS06783.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRZX-ray2.10A1-420[»]
ProteinModelPortalP0A0A5.
SMRP0A0A5. Positions 1-412.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP0A0A5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2348.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15453.

Family and domain databases

Gene3D3.40.630.30. 3 hits.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR003447. Methicillin-R.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamPF02388. FemAB. 1 hit.
[Graphical view]
SUPFAMSSF46589. SSF46589. 1 hit.
SSF55729. SSF55729. 3 hits.
PROSITEPS51191. FEMABX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A0A5.

Entry information

Entry nameFEMA_STAAU
AccessionPrimary (citable) accession number: P0A0A5
Secondary accession number(s): P14304
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: April 18, 2006
Last modified: June 11, 2014
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references