ID   FEMX_STAHJ              Reviewed;         419 AA.
AC   Q4L8C6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
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, fmtB; OrderedLocusNames=SH0790;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; AP006716; BAE04099.1; -; Genomic_DNA.
DR   RefSeq; WP_011275113.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8C6; -.
DR   SMR; Q4L8C6; -.
DR   STRING; 279808.SH0790; -.
DR   PRIDE; Q4L8C6; -.
DR   EnsemblBacteria; BAE04099; BAE04099; SH0790.
DR   KEGG; sha:SH0790; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000543; 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   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..419
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000236178"
SQ   SEQUENCE   419 AA;  48468 MW;  FDAD24BA32A6DA1B CRC64;
     MEKMNITNQE HDAFVKAHPN GDLLQLTKWA ETKRLTGWYS KRVAVGEDGE IKGVGQLLFK
     KIPKLPFTLC YVSRGFVTDY SDKAALEQLL EETKKVAKAE KAYAIKIDPD VEVDKGIDAL
     KNLNALGFKH KGFKEGLSKD YIQPRMTMIT PIDKSDEEIF QSFERRNRSK VRLSLKRGTK
     VERSNREGLK NFAELMKITG ERDGFLTRDL SYFQNIYDSL HEDGDAELFL VKLEPKPVLD
     DIDNELKELE SEKTQLQNKY ERKQVKKTKN KLNDVEAKIQ KSIERKDDMT DLLAKHPNGI
     YLSGALLMFA GSKSYYLYGA SSNDYRDFLP NHHMQYEMMK FAREHGAKTY DFGGTDNNPD
     KDSEHYGLWA FKRVWGTYLS EKIGEFDYVL NQPLYQLIEQ VKPRLTKAKI KISRKLKGK