FEMB_STAA8
ID FEMB_STAA8 Reviewed; 419 AA.
AC Q2FYR1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=SAOUHSC_01374;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION.
RX PubMed=8981974; DOI=10.1128/jb.179.1.9-16.1997;
RA Stranden A.M., Ehlert K., Labischinski H., Berger-Baechi B.;
RT "Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in
RT a femAB null mutant of methicillin-resistant Staphylococcus aureus.";
RL J. Bacteriol. 179:9-16(1997).
RN [3]
RP FUNCTION.
RX PubMed=9393725; DOI=10.1128/jb.179.23.7573-7576.1997;
RA Ehlert K., Schroeder W., Labischinski H.;
RT "Specificities of FemA and FemB for different glycine residues: FemB cannot
RT substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain
RT formation.";
RL J. Bacteriol. 179:7573-7576(1997).
RN [4]
RP SUBUNIT, AND INTERACTION WITH FEMA.
RX PubMed=14523106; DOI=10.1099/mic.0.26315-0;
RA Rohrer S., Berger-Baechi B.;
RT "Application of a bacterial two-hybrid system for the analysis of protein-
RT protein interactions between femABX family proteins.";
RL Microbiology 149:2733-2738(2003).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15228543; DOI=10.1111/j.1365-2958.2004.04149.x;
RA Schneider T., Senn M.M., Berger-Baechi B., Tossi A., Sahl H.-G.,
RA Wiedemann I.;
RT "In vitro assembly of a complete, pentaglycine interpeptide bridge
RT containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus.";
RL Mol. Microbiol. 53:675-685(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.
CC {ECO:0000269|PubMed:15228543, ECO:0000269|PubMed:8981974,
CC ECO:0000269|PubMed:9393725}.
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 Evidence={ECO:0000269|PubMed:15228543};
CC -!- SUBUNIT: Homodimer. Interacts with FemA (Probable).
CC {ECO:0000305|PubMed:14523106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Since cross-linking between the peptide strands is
CC critical for maintaining stability of the cell wall, FemB is a
CC potential target for the development of new antibacterial agents.
CC -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR EMBL; CP000253; ABD30469.1; -; Genomic_DNA.
DR RefSeq; WP_000673098.1; NZ_LS483365.1.
DR RefSeq; YP_499901.1; NC_007795.1.
DR AlphaFoldDB; Q2FYR1; -.
DR SMR; Q2FYR1; -.
DR STRING; 1280.SAXN108_1391; -.
DR EnsemblBacteria; ABD30469; ABD30469; SAOUHSC_01374.
DR GeneID; 3920783; -.
DR KEGG; sao:SAOUHSC_01374; -.
DR PATRIC; fig|93061.5.peg.1258; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_1_0_9; -.
DR OMA; GPYAMHW; -.
DR PRO; PR:Q2FYR1; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Aminoacyltransferase FemB"
FT /id="PRO_0000247018"
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
