FEMA_STAAC
ID FEMA_STAAC Reviewed; 420 AA.
AC Q5HG45;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=SACOL1410;
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).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=7590176; DOI=10.1111/j.1574-6968.1995.tb07837.x;
RA Johnson S., Krueger D., Labischinski H.;
RT "FemA of Staphylococcus aureus: isolation and immunodetection.";
RL FEMS Microbiol. Lett. 132:221-228(1995).
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. Involved in resistance to methicillin (By similarity).
CC {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:0000269|PubMed:7590176}.
CC -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW38155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000046; AAW38155.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000673309.1; NC_002951.2.
DR AlphaFoldDB; Q5HG45; -.
DR SMR; Q5HG45; -.
DR EnsemblBacteria; AAW38155; AAW38155; SACOL1410.
DR KEGG; sac:SACOL1410; -.
DR HOGENOM; CLU_048411_1_0_9; -.
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: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 GO; GO:0046677; P:response to antibiotic; 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; Antibiotic resistance; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Transferase.
FT CHAIN 1..420
FT /note="Aminoacyltransferase FemA"
FT /id="PRO_0000204734"
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