ID Q9ZFG5_STACP Unreviewed; 417 AA.
AC Q9ZFG5;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 03-MAY-2023, entry version 78.
DE RecName: Full=Aminoacyltransferase FemA {ECO:0000256|ARBA:ARBA00016236};
DE EC=2.3.2.17 {ECO:0000256|ARBA:ARBA00012466};
DE AltName: Full=Factor essential for expression of methicillin resistance A {ECO:0000256|ARBA:ARBA00032233};
DE AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase {ECO:0000256|ARBA:ARBA00030706};
GN Name=femA {ECO:0000313|EMBL:AAC69633.1};
GN Synonyms=femA_2 {ECO:0000313|EMBL:VTR17012.1};
GN ORFNames=NCTC11045_01480 {ECO:0000313|EMBL:VTR17012.1};
OS Staphylococcus capitis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=29388 {ECO:0000313|EMBL:AAC69633.1};
RN [1] {ECO:0000313|EMBL:AAC69633.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC27840 {ECO:0000313|EMBL:AAC69633.1};
RA Vannuffel P., Heusterspreute M., Bouyer M., Philippe M., Gala J.-L.;
RT "Molecular characterization of femA from Staphylococcus hominis,
RT Staphylococcus saprophyticus and Staphylococcus haemolyticus and femA-based
RT discrimination of staphylococcal species.";
RL Res. Microbiol. 0:0-0(1998).
RN [2] {ECO:0000313|EMBL:VTR17012.1, ECO:0000313|Proteomes:UP000403553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11045 {ECO:0000313|EMBL:VTR17012.1,
RC ECO:0000313|Proteomes:UP000403553};
RG Pathogen Informatics;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023962};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; AF099964; AAC69633.1; -; Genomic_DNA.
DR EMBL; CABEEX010000003; VTR17012.1; -; Genomic_DNA.
DR RefSeq; WP_049388949.1; NZ_VDSO01000001.1.
DR AlphaFoldDB; Q9ZFG5; -.
DR Proteomes; UP000403553; Unassembled WGS sequence.
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 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:VTR17012.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Transferase {ECO:0000313|EMBL:VTR17012.1}.
FT COILED 249..310
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 417 AA; 49034 MW; C5B6F1BF30B62009 CRC64;
MKFTNLTAKE FSDFTDQMPY SHFTQMEGNY ELKVAEGTDS HLVGIKNNDN QVIAACLLTA
VPVMKIFKYF YSNRGPVIDY DNKELVHFFF NELSKYVKKH NCLYLRVDPY LPYQYLNHDG
EIIGNAGHDW FFNKMEELGF EHEGFHKGFH PILQVRYHSV LDLKDKTAKD VLKGMDSLRK
RNTKKVQKNG VKVRFLSEDE LPIFRSFMED TTETKEFADR DDSFYYNRLK YFKDRVLVPL
AYVDFDEYIE ELNNERDVLN KDLNKALKDI EKRPDNKKAY NKRDNLQQQL DANQQKIDEA
KNLQQEHGNE LPISAGYFFI NPFEVVYYAG GTSNRYRHYA GSYAIQWKMI NYALEHGINR
YNFYGVSGDF SEDAEDVGVI KFKKGYNADV IEYVGDFIKP INKPMYAIYN ALKKLKK
//
