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FEMB_STAEQ
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   25-MAY-2022, entry version 93.
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; Staphylococcaceae;
OC   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., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   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 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; CP000029; AAW54350.1; -; Genomic_DNA.
DR   RefSeq; WP_002439665.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPG5; -.
DR   SMR; Q5HPG5; -.
DR   STRING; 176279.SERP0947; -.
DR   EnsemblBacteria; AAW54350; AAW54350; SERP0947.
DR   KEGG; ser:SERP0947; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OMA; GPYAMHW; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT   CHAIN           1..417
FT                   /note="Aminoacyltransferase FemB"
FT                   /id="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
 
 
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