ID   FEMX_STAA8              Reviewed;         421 AA.
AC   Q2FVZ4; Q9RQG7; Q9X4D7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=SAOUHSC_02527;
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 [GENOMIC DNA].
RA   Berger-Baechi B., Glanzmann P.J., Rohrer S., Tschierske M.;
RT   "FemX and downstream region.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   FUNCTION.
RX   PubMed=9158720; DOI=10.1089/mdr.1996.2.29;
RA   Kopp U., Roos M., Wecke J., Labischinski H.;
RT   "Staphylococcal peptidoglycan interpeptide bridge biosynthesis: a novel
RT   antistaphylococcal target?";
RL   Microb. Drug Resist. 2:29-41(1996).
RN   [4]
RP   FUNCTION.
RX   PubMed=10430946; DOI=10.1073/pnas.96.16.9351;
RA   Rohrer S., Ehlert K., Tschierske M., Labischinski H., Berger-Baechi B.;
RT   "The essential Staphylococcus aureus gene fmhB is involved in the first
RT   step of peptidoglycan pentaglycine interpeptide formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9351-9356(1999).
RN   [5]
RP   SUBUNIT.
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 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       {ECO:0000269|PubMed:10430946, ECO:0000269|PubMed:15228543,
CC       ECO:0000269|PubMed:9158720}.
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         Evidence={ECO:0000269|PubMed:15228543};
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:14523106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Since cross-linking between the peptide strands is
CC       critical for maintaining stability of the cell wall, FemX 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; AF105976; AAF14182.2; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31542.1; -; Genomic_DNA.
DR   RefSeq; WP_000413865.1; NZ_LS483365.1.
DR   RefSeq; YP_500991.1; NC_007795.1.
DR   PDB; 6SNR; X-ray; 1.62 A; A=1-420.
DR   PDBsum; 6SNR; -.
DR   AlphaFoldDB; Q2FVZ4; -.
DR   SMR; Q2FVZ4; -.
DR   STRING; 1280.SAXN108_2511; -.
DR   EnsemblBacteria; ABD31542; ABD31542; SAOUHSC_02527.
DR   GeneID; 3921117; -.
DR   KEGG; sao:SAOUHSC_02527; -.
DR   PATRIC; fig|93061.5.peg.2279; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
DR   PRO; PR:Q2FVZ4; -.
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: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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Antibiotic resistance; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..421
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000247019"
FT   CONFLICT        102
FT                   /note="A -> T (in Ref. 1; AAF14182)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  48521 MW;  2AD9CCB2BC3DD089 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 KTSEKQAKKA QNMINDAQNK IAKNEDLKRD LEALEKEHPE
     GIYLSGALLM FAGSKSYYLY GASSNEFRDF LPNHHMQYTM MKYAREHGAT TYDFGGTDND
     PDKDSEHYGL WAFKKVWGTY LSEKIGEFDY VLNQPLYQLI EQVKPRLTKA KIKISRKLKR
     K