ID FEMB_STAEQ Reviewed; 417 AA.
AC Q5HPG5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 58.
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=SERP0947;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Catalyzes the incorporation of amino acid(s) into the
CC interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA
CC as amino acid donor (By similarity).
CC -!- CATALYTIC ACTIVITY: N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-
CC lysyl-(N(6)-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-
CC acetylglucosamine + 2 glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-
CC isoglutaminyl-L-lysyl-(N(6)-pentaglycyl)-D-alanyl-D-alanine-
CC diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the FemABX family.
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DR EMBL; CP000029; AAW54350.1; -; Genomic_DNA.
DR RefSeq; YP_188525.1; NC_002976.3.
DR ProteinModelPortal; Q5HPG5; -.
DR STRING; 176279.SERP0947; -.
DR EnsemblBacteria; AAW54350; AAW54350; SERP0947.
DR GeneID; 3242013; -.
DR KEGG; ser:SERP0947; -.
DR PATRIC; 19612765; VBIStaEpi130894_0925.
DR eggNOG; COG2348; -.
DR HOGENOM; HOG000280006; -.
DR KO; K11695; -.
DR OMA; DFYKPIN; -.
DR ProtClustDB; CLSK885230; -.
DR BioCyc; SEPI176279:GJJB-973-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016755; F:transferase activity, transferring amino-acyl groups; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 3.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; Methicillin-R.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
KW Complete proteome; Cytoplasm; Peptidoglycan synthesis; Transferase.
FT CHAIN 1 417 Aminoacyltransferase FemB.
FT /FTId=PRO_0000204746.
SQ SEQUENCE 417 AA; 49345 MW; 27A8BAEF93B2F1C9 CRC64;
MKFTELTVKE FENFVQNPSL ESHYFQVKEN IATRESDGFQ 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
//
