FEMA_STAES
ID FEMA_STAES Reviewed; 417 AA.
AC Q8CPA9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, 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=SE_1057;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04654.1; -; Genomic_DNA.
DR RefSeq; NP_764612.1; NC_004461.1.
DR RefSeq; WP_001830979.1; NZ_WBME01000002.1.
DR AlphaFoldDB; Q8CPA9; -.
DR SMR; Q8CPA9; -.
DR STRING; 176280.SE_1057; -.
DR EnsemblBacteria; AAO04654; AAO04654; SE_1057.
DR GeneID; 50018817; -.
DR KEGG; sep:SE_1057; -.
DR PATRIC; fig|176280.10.peg.1033; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_1_0_9; -.
DR OMA; YNFLGIM; -.
DR Proteomes; UP000001411; 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; Transferase.
FT CHAIN 1..417
FT /note="Aminoacyltransferase FemA"
FT /id="PRO_0000232603"
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