ID   FEMB_STAAB              Reviewed;         419 AA.
AC   Q2YXZ4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=SAB1230;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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 (By similarity). {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; AJ938182; CAI80919.1; -; Genomic_DNA.
DR   RefSeq; WP_000673100.1; NC_007622.1.
DR   AlphaFoldDB; Q2YXZ4; -.
DR   SMR; Q2YXZ4; -.
DR   KEGG; sab:SAB1230; -.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OMA; GPYAMHW; -.
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..419
FT                   /note="Aminoacyltransferase FemB"
FT                   /id="PRO_0000232604"
SQ   SEQUENCE   419 AA;  49666 MW;  5D15B6182D5EBBAC 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
     LSKTDGSILN LASGVYFANA YEVNYFSGGS SEKYNQFMGP YMMHWFMINY CFDNGYDRYN
     FYGLSGDFTE NSEDYGVYRF KRGFNVQIEE LIGDFYKPIH KVKYWLFTTL DKLRKKLKK