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Protein

Aminoacyltransferase FemA

Gene

femA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

GO - Molecular functioni

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-15453.
BRENDAi2.3.2.17. 3352.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:femA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002047351 – 420Aminoacyltransferase FemAAdd BLAST420

Interactioni

Subunit structurei

Homodimer. Interacts with FemB (By similarity).By similarity

Protein-protein interaction databases

STRINGi93062.SACOL1410.

Structurei

Secondary structure

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi8 – 16Combined sources9
Helixi27 – 35Combined sources9
Beta strandi39 – 46Combined sources8
Beta strandi52 – 63Combined sources12
Turni64 – 66Combined sources3
Beta strandi67 – 71Combined sources5
Helixi83 – 98Combined sources16
Turni99 – 101Combined sources3
Beta strandi102 – 107Combined sources6
Beta strandi112 – 116Combined sources5
Beta strandi122 – 125Combined sources4
Helixi130 – 137Combined sources8
Beta strandi151 – 153Combined sources3
Beta strandi156 – 162Combined sources7
Helixi168 – 173Combined sources6
Helixi177 – 187Combined sources11
Beta strandi192 – 195Combined sources4
Helixi198 – 200Combined sources3
Helixi201 – 207Combined sources7
Helixi222 – 232Combined sources11
Helixi233 – 235Combined sources3
Beta strandi239 – 244Combined sources6
Helixi245 – 272Combined sources28
Helixi277 – 307Combined sources31
Beta strandi309 – 320Combined sources12
Beta strandi325 – 332Combined sources8
Helixi334 – 339Combined sources6
Helixi341 – 355Combined sources15
Beta strandi360 – 365Combined sources6
Helixi377 – 384Combined sources8
Turni385 – 387Combined sources3
Beta strandi389 – 393Combined sources5
Beta strandi397 – 402Combined sources6
Helixi403 – 411Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRZX-ray2.10A1-420[»]
ProteinModelPortaliP0A0A5.
SMRiP0A0A5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A0A5.

Family & Domainsi

Sequence similaritiesi

Belongs to the FemABX family.Curated

Phylogenomic databases

eggNOGiENOG4108RMH. Bacteria.
COG2348. LUCA.

Family and domain databases

Gene3Di3.40.630.30. 3 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR003447. FEMABX.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02388. FemAB. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
SSF55729. SSF55729. 3 hits.
PROSITEiPS51191. FEMABX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A0A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN
60 70 80 90 100
EVIAACLLTA VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH
110 120 130 140 150
RCLYLHIDPY LPYQYLNHDG EITGNAGNDW FFDKMSNLGF EHTGFHKGFD
160 170 180 190 200
PVLQIRYHSV LDLKDKTADD IIKNMDGLRK RNTKKVKKNG VKVRFLSEEE
210 220 230 240 250
LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL AYINFDEYIK
260 270 280 290 300
ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
310 320 330 340 350
KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI
360 370 380 390 400
NYALNHGIDR YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP
410 420
INKPVYAAYT ALKKVKDRIF
Length:420
Mass (Da):49,124
Last modified:April 18, 2006 - v2
Checksum:iE6790BD7C8B50297
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17688 Genomic DNA. Translation: CAA35679.1. Different initiation.
PIRiS06783.
RefSeqiWP_000673309.1. NZ_MAQP01000001.1.

Genome annotation databases

GeneIDi28381050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17688 Genomic DNA. Translation: CAA35679.1. Different initiation.
PIRiS06783.
RefSeqiWP_000673309.1. NZ_MAQP01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRZX-ray2.10A1-420[»]
ProteinModelPortaliP0A0A5.
SMRiP0A0A5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28381050.

Phylogenomic databases

eggNOGiENOG4108RMH. Bacteria.
COG2348. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15453.
BRENDAi2.3.2.17. 3352.

Miscellaneous databases

EvolutionaryTraceiP0A0A5.

Family and domain databases

Gene3Di3.40.630.30. 3 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR003447. FEMABX.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02388. FemAB. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
SSF55729. SSF55729. 3 hits.
PROSITEiPS51191. FEMABX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFEMA_STAAU
AccessioniPrimary (citable) accession number: P0A0A5
Secondary accession number(s): P14304
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: April 18, 2006
Last modified: November 2, 2016
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure

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.