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Database: UniProt
Entry: FEMA_STAA8
LinkDB: FEMA_STAA8
Original site: FEMA_STAA8 
ID   FEMA_STAA8              Reviewed;         420 AA.
AC   Q2FYR2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=SAOUHSC_01373;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15, AND FUNCTION.
RX   PubMed=9393725; DOI=10.1128/jb.179.23.7573-7576.1997;
RA   Ehlert K., Schroeder W., Labischinski H.;
RT   "Specificities of FemA and FemB for different glycine residues: FemB cannot
RT   substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain
RT   formation.";
RL   J. Bacteriol. 179:7573-7576(1997).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7590176; DOI=10.1111/j.1574-6968.1995.tb07837.x;
RA   Johnson S., Krueger D., Labischinski H.;
RT   "FemA of Staphylococcus aureus: isolation and immunodetection.";
RL   FEMS Microbiol. Lett. 132:221-228(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=8981974; DOI=10.1128/jb.179.1.9-16.1997;
RA   Stranden A.M., Ehlert K., Labischinski H., Berger-Baechi B.;
RT   "Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in
RT   a femAB null mutant of methicillin-resistant Staphylococcus aureus.";
RL   J. Bacteriol. 179:9-16(1997).
RN   [5]
RP   SUBUNIT, AND INTERACTION WITH FEMB.
RX   PubMed=14523106; DOI=10.1099/mic.0.26315-0;
RA   Rohrer S., Berger-Baechi B.;
RT   "Application of a bacterial two-hybrid system for the analysis of protein-
RT   protein interactions between femABX family proteins.";
RL   Microbiology 149:2733-2738(2003).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15228543; DOI=10.1111/j.1365-2958.2004.04149.x;
RA   Schneider T., Senn M.M., Berger-Baechi B., Tossi A., Sahl H.-G.,
RA   Wiedemann I.;
RT   "In vitro assembly of a complete, pentaglycine interpeptide bridge
RT   containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus.";
RL   Mol. Microbiol. 53:675-685(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.
CC       {ECO:0000269|PubMed:15228543, ECO:0000269|PubMed:8981974,
CC       ECO:0000269|PubMed:9393725}.
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         Evidence={ECO:0000269|PubMed:15228543};
CC   -!- SUBUNIT: Homodimer. Interacts with FemB (Probable).
CC       {ECO:0000305|PubMed:14523106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7590176}.
CC   -!- MISCELLANEOUS: Since cross-linking between the peptide strands is
CC       critical for maintaining stability of the cell wall, FemA is a
CC       potential target for the development of new antibacterial agents.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD30468.1; -; Genomic_DNA.
DR   RefSeq; WP_000673309.1; NZ_LS483365.1.
DR   RefSeq; YP_499900.1; NC_007795.1.
DR   AlphaFoldDB; Q2FYR2; -.
DR   SMR; Q2FYR2; -.
DR   STRING; 93061.SAOUHSC_01373; -.
DR   PaxDb; 1280-SAXN108_1390; -.
DR   GeneID; 3920782; -.
DR   KEGG; sao:SAOUHSC_01373; -.
DR   PATRIC; fig|93061.5.peg.1257; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OrthoDB; 2173585at2; -.
DR   PRO; PR:Q2FYR2; -.
DR   Proteomes; UP000008816; 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   Gene3D; 1.20.58.90; -; 1.
DR   Gene3D; 3.40.630.30; -; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR003447; FEMABX.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR36174:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS51191; FEMABX; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW   Peptidoglycan synthesis; Reference proteome; Transferase.
FT   CHAIN           1..420
FT                   /note="Aminoacyltransferase FemA"
FT                   /id="PRO_0000247017"
SQ   SEQUENCE   420 AA;  49124 MW;  E6790BD7C8B50297 CRC64;
     MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA
     VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG
     EITGNAGNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK
     RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL
     AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
     KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR
     YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF
//
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