FEMX_STAAC
ID FEMX_STAAC Reviewed; 421 AA.
AC Q5HDU6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=SACOL2253;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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 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; CP000046; AAW37126.1; -; Genomic_DNA.
DR RefSeq; WP_000413868.1; NC_002951.2.
DR AlphaFoldDB; Q5HDU6; -.
DR SMR; Q5HDU6; -.
DR EnsemblBacteria; AAW37126; AAW37126; SACOL2253.
DR KEGG; sac:SACOL2253; -.
DR HOGENOM; CLU_048411_0_1_9; -.
DR OMA; FGLIQFK; -.
DR Proteomes; UP000000530; 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_0000236170"
SQ SEQUENCE 421 AA; 48551 MW; 6CA87BC800FCDCF1 CRC64;
MEKMHITNQE HDAFVKSHPN GDLLQLTKWA ETKKLTGWYA RRIAVGRDGE VQGVAQLLFK
KVPKLPYTLC YISRGFVVDY SNKEALNALL DSAKEIAKAE KTYAIKIDPD 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