ID   FEMA_STAAB              Reviewed;         420 AA.
AC   Q2YXZ5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 92.
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=SAB1229;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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 (By similarity). {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI80918.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ938182; CAI80918.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000673320.1; NC_007622.1.
DR   AlphaFoldDB; Q2YXZ5; -.
DR   SMR; Q2YXZ5; -.
DR   KEGG; sab:SAB1229; -.
DR   HOGENOM; CLU_048411_1_0_9; -.
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..420
FT                   /note="Aminoacyltransferase FemA"
FT                   /id="PRO_0000232597"
SQ   SEQUENCE   420 AA;  49200 MW;  2F070DE00B595A3F CRC64;
     MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA
     VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG
     EITGNASNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK
     RNTKKVKKNG VKVRYLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL
     AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
     KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR
     YNFYGVSGKF TEDAEDTGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF