ID   FEMX_STAAW              Reviewed;         421 AA.
AC   Q8NVA9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Lipid II:glycine glycyltransferase;
DE            EC=2.3.2.16;
DE   AltName: Full=Factor essential for expression of methicillin resistance X;
GN   Name=femX; Synonyms=fmhB; OrderedLocusNames=MW2180;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the incorporation of the first glycine of the
CC       pentaglycine interpeptide bridge, which is characteristic of the
CC       S.aureus peptidoglycan. This glycine is added to the epsilon-amino
CC       group of the L-lysine of the membrane-bound lipid II intermediate
CC       (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala-D-
CC       Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in
CC       a ribosome-independent mechanism. Involved in methicillin resistance
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-
CC         Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + glycyl-
CC         tRNA(Gly) = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-
CC         Lys-(N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
CC         diphosphate + H(+) + tRNA(Gly); Xref=Rhea:RHEA:30435, Rhea:RHEA-
CC         COMP:9664, Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62233,
CC         ChEBI:CHEBI:62234, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.16;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB96045.1; -; Genomic_DNA.
DR   RefSeq; WP_000413863.1; NC_003923.1.
DR   AlphaFoldDB; Q8NVA9; -.
DR   SMR; Q8NVA9; -.
DR   EnsemblBacteria; BAB96045; BAB96045; BAB96045.
DR   KEGG; sam:MW2180; -.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016755; F:aminoacyltransferase activity; 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   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS51191; FEMABX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW   Transferase.
FT   CHAIN           1..421
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000236175"
SQ   SEQUENCE   421 AA;  48522 MW;  F9C0F8E6361DD82B CRC64;
     MEKMHITNQE HDAFVKSHPN GDLLQLTKWA ETKKLTGWYA RRIAVGRDGE VQGVAQLLFK
     KVPKLPYTLC YISRGFVVDY SNKEALNALL DSAKEIAKAE KAYAIKIDPD VEVDKGTDAL
     QNLKALGFKH KGFKEGLSKD YIQPRMTMIT PIDKNDDELL NSFERRNRSK VRLALKRGTT
     VERSDREGLK TFAELMKITG ERDGFLTRDI SYFENIYDAL HEDGDAELFL VKLDPKENIA
     KVNQELNELH AEIAKWQQKM ETSEKQAKKA QNMINDAQNK IAKNEDLKRD LEALEKEHPE
     GIYLSGALLM FAGSKSYYLY GASSNEFRDF LPNHHMQYTM MKYAREHGAT TYDFGGTDND
     PDKDSEHYGL WAFKKVWGTY LSEKIGEFDY VLNQPLYQLI EQVKPRLTKA KIKISRKLKR
     K