ID   FEMX_STAAB              Reviewed;         421 AA.
AC   Q2YYN5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=SAB2134c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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 (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; AJ938182; CAI81823.1; -; Genomic_DNA.
DR   RefSeq; WP_000413857.1; NC_007622.1.
DR   AlphaFoldDB; Q2YYN5; -.
DR   SMR; Q2YYN5; -.
DR   KEGG; sab:SAB2134c; -.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
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   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; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Peptidoglycan synthesis; Transferase.
FT   CHAIN           1..421
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000236168"
SQ   SEQUENCE   421 AA;  48552 MW;  13F3FE359FC6BA22 CRC64;
     MEKMHITNQE HDAFVKSHPN GDLLQLTKWA ETKKLTGWYA RRIAVGRDGE IQGVAQLLFK
     KVPKLPYTLC YISRGFVVDY SNKEALNALL DSAKEIAKAE KAYAIKIDPD VEVDKGTDAL
     QNLKALGFKH KGFKEGLSKD YIQPRMTMIT PIDKNDDELL NSYERRNRSK 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