ID A1XFE3_STAAU Unreviewed; 405 AA.
AC A1XFE3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 03-MAY-2023, entry version 53.
DE RecName: Full=Aminoacyltransferase FemA {ECO:0000256|ARBA:ARBA00016236};
DE EC=2.3.2.17 {ECO:0000256|ARBA:ARBA00012466};
DE AltName: Full=Factor essential for expression of methicillin resistance A {ECO:0000256|ARBA:ARBA00032233};
DE AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase {ECO:0000256|ARBA:ARBA00030706};
DE Flags: Fragment;
GN Name=femA {ECO:0000313|EMBL:ABC75743.1};
OS Staphylococcus aureus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:ABC75743.1};
RN [1] {ECO:0000313|EMBL:ABC75743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RPH2-R11 {ECO:0000313|EMBL:ABC75744.1}, and SJOG 30-R3
RC {ECO:0000313|EMBL:ABC75743.1};
RX PubMed=17715374; DOI=10.1128/JCM.01082-07;
RA Cai Y., Kong F., Wang Q., Tong Z., Sintchenko V., Zeng X., Gilbert G.L.;
RT "Comparison of single- and multilocus sequence typing and toxin gene
RT profiling for characterization of methicillin-resistant Staphylococcus
RT aureus.";
RL J. Clin. Microbiol. 45:3302-3308(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-
CC (N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate +
CC 2 glycyl-tRNA(Gly) = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-
CC (N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-
CC GlcNAc + 2 tRNA(Gly); Xref=Rhea:RHEA:30439, Rhea:RHEA-COMP:9664,
CC Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62234,
CC ChEBI:CHEBI:62235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00023962};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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; DQ352457; ABC75743.1; -; Genomic_DNA.
DR EMBL; DQ352458; ABC75744.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XFE3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; 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 Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR36174:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT COILED 247..304
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC75743.1"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:ABC75743.1"
SQ SEQUENCE 405 AA; 47329 MW; C9DF7C13278CB90A CRC64;
FTNLTAKEFG AFTDSMPYSH FTQTVGHYEL KLAEGYETHL VGIKNNNNEV IAACLLTAVP
VMKVFKYFYS NRGPVIDYEN QELVHFFFNE LSKYVKKHRC LYLHIDPYLP YQYLNHDGEI
TGNAGNDWFF DKMSNLGFEH TGFHKGFDPV LQIRYHSVLD LKDKTADDII KNMDGLRKRN
TKKVKKNGVK VRFLSEEELP IFRSFMEDTS ESKAFADRDD KFYYNRLKYY KDRVLVPLAY
INFDEYIKEL NEERDILNKD LNKALKDIEK RPENKKAHNK RDNLQQQLDA NEQKIEEGKR
LQEEHGNELP ISAGFFFINP FEVVYYAGGT SNAFRHFAGS YAVQWEMINY ALNHGIDRYN
FYGVSGKFTE DAEDAGVVKF KKGYNAEIIE YVGDFIKPIN KPVYA
//
