ID   FEMA_STAEP              Reviewed;         417 AA.
AC   P95734;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 80.
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;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ST335;
RX   PubMed=8973364; DOI=10.1016/s0378-1119(96)00450-7;
RA   Alborn W.E. Jr., Hoskins J., Uenal S., Flokowitsch J.E., Hayes C.A.,
RA   Dotzlaf J.E., Yeh W.K., Skatrud P.L.;
RT   "Cloning and characterization of femA and femB from Staphylococcus
RT   epidermidis.";
RL   Gene 180:177-181(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB41947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U23713; AAB41947.1; ALT_INIT; Genomic_DNA.
DR   PIR; JC5325; JC5325.
DR   AlphaFoldDB; P95734; -.
DR   SMR; P95734; -.
DR   BRENDA; 2.3.2.17; 5875.
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; Transferase.
FT   CHAIN           1..417
FT                   /note="Aminoacyltransferase FemA"
FT                   /id="PRO_0000232602"
SQ   SEQUENCE   417 AA;  48929 MW;  18132C16BC26732C CRC64;
     MKFANLTAKE FSDFTDRMTY SHFTQMEGNY ELKVAEGTES HLVGIKNNDN EVIAACLLTA
     VPVMKIFKYF YSNRGPVIDY NNKELVHFFF NELSKYVKKY NCLYLRVDPY LPYQYLNHEG
     EITGNAGHDW IFDELESLGY KHEGFHKGFD PVLQIRYHSV LNLANKSAND VLKNMDGLRK
     RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSETKDFADR EDSFYYNRFK HYKGRVLVPL
     AYINFDEYIE ELNNERNVLN KDYNKALKDI EKRPENKKAH NKKENLEQQL DANQQKINEA
     KNLKQEHGNE LPISAGFFII NPFEVVYYAG GTSNRYRHFA GSYAVQWKMI NYAIEHGINR
     YNFYGISGDF SEDAEDAGVV KFKKGYDADV IEYVGDFIKP INKPMYNIYR TLKKLKK