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 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=SAOUHSC_01373;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; 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; 1280.SAXN108_1390; -.
DR EnsemblBacteria; ABD30468; ABD30468; SAOUHSC_01373.
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 OMA; YNFLGIM; -.
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 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 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
