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P0A0A5

- FEMA_STAAU

UniProt

P0A0A5 - FEMA_STAAU

Protein

Aminoacyltransferase FemA

Gene

femA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 2 (18 Apr 2006)
      Previous versions | rss
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    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

    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

    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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A0A5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FemABX family.Curated

    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: October 1, 2014
    This is version 54 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