ID   FEMA_STAAR              Reviewed;         420 AA.
AC   Q6GH31;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Aminoacyltransferase FemA;
DE            EC=2.3.2.17;
DE   AltName: Full=Factor essential for expression of methicillin resistance A;
DE   AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
GN   Name=femA; OrderedLocusNames=SAR1387;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the formation of the pentaglycine interpeptide
CC       bridge, which is characteristic of the S.aureus peptidoglycan. Adds
CC       glycines 2 and 3 of the pentaglycine bridge, using glycyl-tRNA(Gly) as
CC       donor. Involved in resistance to methicillin (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-
CC         (N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate +
CC         2 glycyl-tRNA(Gly) = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-
CC         (N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-
CC         GlcNAc + 2 tRNA(Gly); Xref=Rhea:RHEA:30439, Rhea:RHEA-COMP:9664,
CC         Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62234,
CC         ChEBI:CHEBI:62235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.17;
CC   -!- SUBUNIT: Homodimer. Interacts with FemB (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG40385.1; -; Genomic_DNA.
DR   RefSeq; WP_000673317.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH31; -.
DR   SMR; Q6GH31; -.
DR   KEGG; sar:SAR1387; -.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OMA; YNFLGIM; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR003447; FEMABX.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS51191; FEMABX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW   Transferase.
FT   CHAIN           1..420
FT                   /note="Aminoacyltransferase FemA"
FT                   /id="PRO_0000232598"
SQ   SEQUENCE   420 AA;  49154 MW;  DF199ADE792F9094 CRC64;
     MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA
     VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG
     EITGNAGNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK
     RNTKKVKKNG VKVRYLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKERVLVPL
     AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
     KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR
     YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF