ID   FEMB_STAAR              Reviewed;         419 AA.
AC   Q6GH30;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Aminoacyltransferase FemB;
DE            EC=2.3.2.18;
DE   AltName: Full=Factor essential for expression of methicillin resistance B;
DE   AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
GN   Name=femB; OrderedLocusNames=SAR1388;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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 4 and 5 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=2 glycyl-tRNA(Gly) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-
CC         tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-GlcNAc
CC         = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-penta-Gly)-D-Ala-
CC         D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-GlcNAc + 2 tRNA(Gly);
CC         Xref=Rhea:RHEA:30443, Rhea:RHEA-COMP:9664, Rhea:RHEA-COMP:9683,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:62235, ChEBI:CHEBI:62236,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.18;
CC   -!- SUBUNIT: Homodimer. Interacts with FemA (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; BX571856; CAG40386.1; -; Genomic_DNA.
DR   RefSeq; WP_000673098.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH30; -.
DR   SMR; Q6GH30; -.
DR   KEGG; sar:SAR1388; -.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OMA; GPYAMHW; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000596; 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..419
FT                   /note="Aminoacyltransferase FemB"
FT                   /id="PRO_0000204741"
SQ   SEQUENCE   419 AA;  49676 MW;  9C5C90C340E86288 CRC64;
     MKFTELTVTE FDNFVQNPSL ESHYFQVKEN IVTRENDGFE VVLLGIKDDN NKVIAASLFS
     KIPTMGSYVY YSNRGPVMDF SDLGLVDYYL KELDKYLQQH QCLYVKLDPY WLYHLYDKDI
     VPFEGREKND ALVNLFKSHG YEHHGFTTEY DTSSQVRWMG VLNLEGKTPE TLKKTFDSQR
     KRNINKAINY GVKVRFLERD EFNLFLDLYR ETEERAGFVS KTDDYFYNFI DTYGDKVLVP
     LAYIDLDEYV LKLQQELNDK ENRRDQMMAK ENKSDKQMKK IAELDKQIDH DQHELLNASE
     LSKTDGPILN LASGVYFANA YEVNYFSGGS SEKYNQFMGP YMMHWFMINY CFDNGYDRYN
     FYGLSGDFTE NSEDYGVYRF KRGFNVQIEE LIGDFYKPIH KVKYWLFTTL DKLRKKLKK