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MURE_STAAC
ID   MURE_STAAC              Reviewed;         493 AA.
AC   O86491; Q5HH68;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.7 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=L-lysine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; OrderedLocusNames=SACOL1023;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9650993; DOI=10.1089/mdr.1998.4.85;
RA   Ludovice A.M., Wu S.-W., de Lencastre H.;
RT   "Molecular cloning and DNA sequencing of the Staphylococcus aureus UDP-N-
RT   acetylmuramyl tripeptide synthetase (murE) gene, essential for the optimal
RT   expression of methicillin resistance.";
RL   Microb. Drug Resist. 4:85-90(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
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 addition of L-lysine to the nucleotide
CC       precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC       biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-
CC       Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanyl-gamma-D-glutamyl-L-lysine; Xref=Rhea:RHEA:17969,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83903,
CC         ChEBI:CHEBI:456216; EC=6.3.2.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
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DR   EMBL; Y14370; CAA74740.1; -; Genomic_DNA.
DR   EMBL; CP000046; AAW36489.1; -; Genomic_DNA.
DR   RefSeq; WP_000340118.1; NC_002951.2.
DR   AlphaFoldDB; O86491; -.
DR   SMR; O86491; -.
DR   EnsemblBacteria; AAW36489; AAW36489; SACOL1023.
DR   KEGG; sac:SACOL1023; -.
DR   HOGENOM; CLU_022291_0_1_9; -.
DR   OMA; CFMEVSS; -.
DR   BioCyc; MetaCyc:MON-12253; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00208; MurE; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   SUPFAM; SSF63418; SSF63418; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..493
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine
FT                   ligase"
FT                   /id="PRO_0000101940"
FT   MOTIF           406..409
FT                   /note="L-lysine recognition motif"
FT   BINDING         30
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         152..153
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         179
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         187
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   CONFLICT        2..5
FT                   /note="DAST -> QVRC (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="G -> S (in Ref. 1; CAA74740)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  54105 MW;  0D224B23DA5A1390 CRC64;
     MDASTLFKKV KVKRVLGSLE QQIDDITTDS RTAREGSIFV ASVGYTVDSH KFCQNVADQG
     CKLVVVNKEQ SLPANVTQVV VPDTLRVASI LAHTLYDYPS HQLVTFGVTG TNGKTSIATM
     IHLIQRKLQK NSAYLGTNGF QINETKTKGA NTTPETVSLT KKIKEAVDAG AESMTLEVSS
     HGLVLGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYVVLNN
     DDSFSEYLRT VTPYEVFSYG IDEEAQFMAK NIQESLQGVS FDFVTPFGTY PVKSPYVGKF
     NISNIMAAMI AVWSKGTSLE TIIKAVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK
     LIDAVQPFVK QKLIFLVGMA GERDLTKTPE MGRVACRADY VIFTPDNPAN DDPKMLTAEL
     AKGATHQNYI EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL
     EAAYKKFGGG PVD
 
 
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