ID   FEMX_STAEQ              Reviewed;         416 AA.
AC   Q5HLY6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=SERP1844;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW55189.1; -; Genomic_DNA.
DR   RefSeq; WP_002438530.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLY6; -.
DR   SMR; Q5HLY6; -.
DR   STRING; 176279.SERP1844; -.
DR   PRIDE; Q5HLY6; -.
DR   EnsemblBacteria; AAW55189; AAW55189; SERP1844.
DR   GeneID; 50018062; -.
DR   KEGG; ser:SERP1844; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT   CHAIN           1..416
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000236176"
SQ   SEQUENCE   416 AA;  47977 MW;  D7FE6BCAA84917B8 CRC64;
     MEKMNITNQQ HDAFVKSHPN GDLLQLSKWA DTKKLTGWYS RRIAVGENGQ IKGVGQLLFK
     KIPKLPYTLC YVSRGFVADY NNKEVLEALL SYAKEVAKDE KSYAIKIDPD VEVDKGAEAL
     KNLRELGFKH KGFKEGLSKD YIQPRMTMIT PIDKTDDELV QSFERRNRSK VRLALKRGTK
     VERSNREGLK IFANLMKITG ERDGFLTRDI SYFENIYDAL HEDGDAELFL VKLEPKPVLD
     TVNQDLEAQL AEKEKLQSKK QDKKTLNKLN DIDNKIKKTN ELKSDLTELE KSEPEGIYLS
     GALLMFAGNK SYYLYGASSN DYRDFLPNHH MQFEMMKYAR EHGATTYDFG GTDNDPDKDS
     EHYGLWAFKR VWGTYLSEKI GEFDYVLNQP LYHLVEKVKP RLTKAKIKIS RKLKGK