FEMX_STAAR
ID FEMX_STAAR Reviewed; 421 AA.
AC Q6GEH2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=SAR2346;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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 (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; BX571856; CAG41327.1; -; Genomic_DNA.
DR RefSeq; WP_000413875.1; NC_002952.2.
DR AlphaFoldDB; Q6GEH2; -.
DR SMR; Q6GEH2; -.
DR KEGG; sar:SAR2346; -.
DR HOGENOM; CLU_048411_0_1_9; -.
DR OMA; FGLIQFK; -.
DR OrthoDB; 891566at2; -.
DR Proteomes; UP000000596; 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 3: Inferred from homology;
KW Acyltransferase; Antibiotic resistance; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Transferase.
FT CHAIN 1..421
FT /note="Lipid II:glycine glycyltransferase"
FT /id="PRO_0000236173"
SQ SEQUENCE 421 AA; 48513 MW; 240999083743D556 CRC64;
MEKMHITNQE HDAFVKSNPN GDLLQLTKWA ETKKLTGWYA RRIAVGRDGE IQGVAQLLFK
KVPKLPYTLC YISRGFVVDY SNKEALNALL DSAKEIAKAE KAYAIKIDPD VEVDKGTDAL
QNLKALGFKH KGFKEGLSKD YIQPRMTMIT PIDKNDDELL NSFERRNRSK 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