ID   FEMA_STAEQ              Reviewed;         417 AA.
AC   Q5HPG6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=SERP0946;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the incorporation of amino acid(s) into the
CC       interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA as
CC       amino acid donor. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; CP000029; AAW54349.1; -; Genomic_DNA.
DR   RefSeq; WP_001830979.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPG6; -.
DR   SMR; Q5HPG6; -.
DR   STRING; 176279.SERP0946; -.
DR   EnsemblBacteria; AAW54349; AAW54349; SERP0946.
DR   GeneID; 50018817; -.
DR   KEGG; ser:SERP0946; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OMA; YNFLGIM; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000531; 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   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; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Peptidoglycan synthesis; Reference proteome; Transferase.
FT   CHAIN           1..417
FT                   /note="Aminoacyltransferase FemA"
FT                   /id="PRO_0000204737"
SQ   SEQUENCE   417 AA;  49017 MW;  B36B9917B5942C0A CRC64;
     MKFTNLTAKE FSDFTDRMTY SHFTQMEGNY ELKVAEGTES HLVGIKNNDN EVIAACLLTA
     VPVMKIFKYF YSNRGPVIDY NNKELVHFFF NELSKYVKKY NCLYLRVDPY LPYQYLNHEG
     EITGNAGHDW IFDELESLGY KHEGFHKGFD PVLQIRYHSV LNLANKSAND VLKNMDGLRK
     RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSETKDFADR EDSFYYNRFK HYKDRVLVPL
     AYINFDEYIE ELNNERNVLN KDYNKALKDI EKRPENKKAH NKKENLEQQL DANQQKINEA
     KNLKQEHGNE LPISAGFFII NPFEVVYYAG GTSNRYRHFA GSYAVQWKMI NYAIEHGINR
     YNFYGISGDF SEDAEDAGVV KFKKGYDADV IEYVGDFIKP INKPMYNIYR TLKKLKK