FEMX_STAES
ID FEMX_STAES Reviewed; 416 AA.
AC Q8CNE9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=SE_1835;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO05476.1; -; Genomic_DNA.
DR RefSeq; NP_765390.1; NC_004461.1.
DR RefSeq; WP_002438530.1; NZ_WBME01000007.1.
DR AlphaFoldDB; Q8CNE9; -.
DR SMR; Q8CNE9; -.
DR STRING; 176280.SE_1835; -.
DR EnsemblBacteria; AAO05476; AAO05476; SE_1835.
DR GeneID; 50018062; -.
DR KEGG; sep:SE_1835; -.
DR PATRIC; fig|176280.10.peg.1791; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_0_1_9; -.
DR OMA; FGLIQFK; -.
DR Proteomes; UP000001411; 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..416
FT /note="Lipid II:glycine glycyltransferase"
FT /id="PRO_0000236177"
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
