FEMX_STAAU
ID FEMX_STAAU Reviewed; 421 AA.
AC P0C1Q0; Q9RQG7; Q9X4D7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 55748;
RX PubMed=10077832; DOI=10.1111/j.1574-6968.1999.tb13417.x;
RA Tschierske M., Mori C., Rohrer S., Ehlert K., Shaw K.J., Berger-Baechi B.;
RT "Identification of three additional femAB-like open reading frames in
RT Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 171:97-102(1999).
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 (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; AF106850; AAD23961.1; -; Genomic_DNA.
DR RefSeq; WP_000413862.1; NZ_WYDB01000006.1.
DR AlphaFoldDB; P0C1Q0; -.
DR SMR; P0C1Q0; -.
DR OMA; FGLIQFK; -.
DR BRENDA; 2.3.2.16; 3352.
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..421
FT /note="Lipid II:glycine glycyltransferase"
FT /id="PRO_0000236167"
SQ SEQUENCE 421 AA; 48536 MW; 7250F8E6361DC6DA CRC64;
MEKMHITNQE HDAFVKSHPN GDLLQLTKWA ETKKLTGWYA RRIAVGRDGE VQGVAQLLFK
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 ILNQPLYQLI EQVKPRLTKA KIKISRKLKR
K