ID   FEMB_STAEP              Reviewed;         417 AA.
AC   P95735;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 72.
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;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ST335;
RX   PubMed=8973364; DOI=10.1016/s0378-1119(96)00450-7;
RA   Alborn W.E. Jr., Hoskins J., Uenal S., Flokowitsch J.E., Hayes C.A.,
RA   Dotzlaf J.E., Yeh W.K., Skatrud P.L.;
RT   "Cloning and characterization of femA and femB from Staphylococcus
RT   epidermidis.";
RL   Gene 180:177-181(1996).
CC   -!- FUNCTION: Catalyzes the incorporation of amino acid(s) into the
CC       interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA as
CC       amino acid donor. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; U23714; AAB41948.1; -; Genomic_DNA.
DR   PIR; JC5326; JC5326.
DR   AlphaFoldDB; P95735; -.
DR   SMR; P95735; -.
DR   BRENDA; 2.3.2.18; 5875.
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..417
FT                   /note="Aminoacyltransferase FemB"
FT                   /id="PRO_0000232605"
SQ   SEQUENCE   417 AA;  49287 MW;  0B4947C373830D29 CRC64;
     MKFTELTVKE FENFVQNPSL ESHYFQVKEN IATRESDGFQ VVLLGVKDDD NRVIAASLFS
     KIPTMGSYVY YSNRGPVMDY SDLGLVDFYL KELDKYLHQH QCLYVKLDPY WLYQVYDKDI
     NPLTEKNDAL VNLFKSHGYD HHGFTTQYDS SSQVRWMGVL DLEGKTPASL RKEFDSQRKR
     NINKAINYGV KVRFLSKDEF GLFLDLYRET EARTGFASKT DDYFYNFIEH YGDKVLVPLA
     YIDLNEYIQH LQESLNDKEN RRDDMMAKEN KTDKQLKKIA ELDKQIDHDK KELLQASELR
     QTDGEILNLA SGVYFANAYE VNYFSGGSSE KYNQYMGPYA MHWHMINYCF DNGYDRYNFY
     GLSGDFTENS EDYGVYRFKR GFNVRIEELI GDFYKPINKV KYWLFNTLDR IRNKLKK