FEMB_STAES
ID FEMB_STAES Reviewed; 417 AA.
AC Q8CPA8;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=SE_1058;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04655.1; -; Genomic_DNA.
DR RefSeq; NP_764613.1; NC_004461.1.
DR RefSeq; WP_002485777.1; NZ_WBME01000002.1.
DR AlphaFoldDB; Q8CPA8; -.
DR SMR; Q8CPA8; -.
DR STRING; 176280.SE_1058; -.
DR EnsemblBacteria; AAO04655; AAO04655; SE_1058.
DR KEGG; sep:SE_1058; -.
DR PATRIC; fig|176280.10.peg.1034; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_1_0_9; -.
DR OMA; GPYAMHW; -.
DR Proteomes; UP000001411; 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 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_0000204745"
SQ SEQUENCE 417 AA; 49357 MW; 087A4C369798CE3A CRC64;
MKFTELTVKE FENFVQNPSL ESHYFQVKEN IAIRESDGFQ VVLLGVKDDD NRVIAASLFS
KIPTMGSYVY YSNRGPVMDY SDLGLVDFYL KELDKYLHQH QCLYVKLDPY WLYQVYDKDI
NPLTEKNDAL VNLFKSHGYD HHGFTTQYDS SSQVRWMGVL DLEGKTPASL RKEFDSQRKR
NINKAINYGV KVRFLSKDEF DLFLDLYRET EARTGFASKT DDYFYNFIEH YGDKVLVPLA
YIDLNEYIQH LQESLNDKEN RRDDMMAKEN KTDKQLKKIA ELDKQIDHDK KELLQASELR
QTDGEILNLA SGVYFANAYE VNYFSGGSSE KYNQYMGPYA MHWHMINYCF DNGYDRYNFY
GLSGDFTENS EDYGVYRFKR GFNVRIEELI GDFYKPINKV KYWLFNTLDR IRNKLKK
