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P0A0A5

- FEMA_STAAU

UniProt

P0A0A5 - FEMA_STAAU

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Protein

Aminoacyltransferase FemA

Gene
femA
Organism
Staphylococcus aureus
Status
Reviewed - 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

  1. nucleotide binding Source: InterPro
  2. transferase activity, transferring amino-acyl groups Source: InterPro

GO - Biological processi

  1. peptidoglycan biosynthetic process Source: UniProtKB-KW
  2. 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-15453.

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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Aminoacyltransferase FemAPRO_0000204735Add
BLAST

Proteomic databases

PRIDEiP0A0A5.

Interactioni

Subunit structurei

Homodimer. Interacts with FemB By similarity.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Helixi8 – 169
Helixi27 – 359
Beta strandi39 – 468
Beta strandi52 – 6312
Turni64 – 663
Beta strandi67 – 715
Helixi83 – 9816
Turni99 – 1013
Beta strandi102 – 1076
Beta strandi112 – 1165
Beta strandi122 – 1254
Helixi130 – 1378
Beta strandi151 – 1533
Beta strandi156 – 1627
Helixi168 – 1736
Helixi177 – 18711
Beta strandi192 – 1954
Helixi198 – 2003
Helixi201 – 2077
Helixi222 – 23211
Helixi233 – 2353
Beta strandi239 – 2446
Helixi245 – 27228
Helixi277 – 30731
Beta strandi309 – 32012
Beta strandi325 – 3328
Helixi334 – 3396
Helixi341 – 35515
Beta strandi360 – 3656
Helixi377 – 3848
Turni385 – 3873
Beta strandi389 – 3935
Beta strandi397 – 4026
Helixi403 – 4119

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRZX-ray2.10A1-420[»]
ProteinModelPortaliP0A0A5.
SMRiP0A0A5. Positions 1-412.

Miscellaneous databases

EvolutionaryTraceiP0A0A5.

Family & Domainsi

Sequence similaritiesi

Belongs to the FemABX family.

Phylogenomic databases

eggNOGiCOG2348.

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

MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN    50
EVIAACLLTA VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH 100
RCLYLHIDPY LPYQYLNHDG EITGNAGNDW FFDKMSNLGF EHTGFHKGFD 150
PVLQIRYHSV LDLKDKTADD IIKNMDGLRK RNTKKVKKNG VKVRFLSEEE 200
LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL AYINFDEYIK 250
ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG 300
KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI 350
NYALNHGIDR YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP 400
INKPVYAAYT ALKKVKDRIF 420
Length:420
Mass (Da):49,124
Last modified:April 18, 2006 - v2
Checksum:iE6790BD7C8B50297
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17688 Genomic DNA. Translation: CAA35679.1. Different initiation.
PIRiS06783.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17688 Genomic DNA. Translation: CAA35679.1 . Different initiation.
PIRi S06783.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LRZ X-ray 2.10 A 1-420 [» ]
ProteinModelPortali P0A0A5.
SMRi P0A0A5. Positions 1-412.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0A0A5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2348.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15453.

Miscellaneous databases

EvolutionaryTracei P0A0A5.

Family and domain databases

Gene3Di 3.40.630.30. 3 hits.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR003447. FEMABX.
IPR010978. tRNA-bd_arm.
[Graphical view ]
Pfami PF02388. FemAB. 1 hit.
[Graphical view ]
SUPFAMi SSF46589. SSF46589. 1 hit.
SSF55729. SSF55729. 3 hits.
PROSITEi PS51191. FEMABX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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: September 3, 2014
This is version 53 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

External Data

Dasty 3

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