FEMA_STAAS
ID FEMA_STAAS Reviewed; 420 AA.
AC Q6G9I5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Aminoacyltransferase FemA;
DE EC=2.3.2.17;
DE AltName: Full=Factor essential for expression of methicillin resistance A;
DE AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
GN Name=femA; OrderedLocusNames=SAS1314;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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 formation of the pentaglycine interpeptide
CC bridge, which is characteristic of the S.aureus peptidoglycan. Adds
CC glycines 2 and 3 of the pentaglycine bridge, using glycyl-tRNA(Gly) as
CC donor (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. Interacts with FemB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR EMBL; BX571857; CAG43091.1; -; Genomic_DNA.
DR RefSeq; WP_000673309.1; NC_002953.3.
DR AlphaFoldDB; Q6G9I5; -.
DR SMR; Q6G9I5; -.
DR KEGG; sas:SAS1314; -.
DR HOGENOM; CLU_048411_1_0_9; -.
DR OMA; YNFLGIM; -.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR InterPro; IPR010978; tRNA-bd_arm.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF46589; SSF46589; 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..420
FT /note="Aminoacyltransferase FemA"
FT /id="PRO_0000232599"
SQ SEQUENCE 420 AA; 49124 MW; E6790BD7C8B50297 CRC64;
MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA
VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG
EITGNAGNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK
RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL
AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR
YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF