(data stored in ACNUC7421 zone)

HOGENOM: STAAM_1_PE1011

ID   STAAM_1_PE1011                       STANDARD;      PRT;   494 AA.
AC   STAAM_1_PE1011; P65479; Q99V74;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
DE   EC=6.3.2 7;AltName: Full=L-lysine-adding enzyme;AltName:
DE   Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase;AltName:
DE   Full=UDP-MurNAc-tripeptide synthetase;AltName:
DE   Full=UDP-N-acetylmuramyl-tripeptide synthetase; (STAAM_1.PE1011).
GN   Name=murE; OrderedLocusNames=SAV1018;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAM_1.PE1011.
CC       Staphylococcus aureus subsp. aureus Mu50, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MURE_STAAM
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-
CC       alanyl-D-glutamyl-L-lysine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC   -!- GENE_FAMILY: HOG000268118 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P65479; Q99V74; -.
DR   EMBL; BA000017; BAB57180.1; -; Genomic_DNA.
DR   RefSeq; NP_371542.1; NC_002758.2.
DR   ProteinModelPortal; P65479; -.
DR   STRING; P65479; -.
DR   World-2DPAGE; 0002:P65479; -.
DR   EnsemblBacteria; EBSTAT00000007708; EBSTAP00000007526; EBSTAG00000007707.
DR   GeneID; 1120993; -.
DR   GenomeReviews; BA000017_GR; SAV1018.
DR   KEGG; sav:SAV1018; -.
DR   eggNOG; COG0769; -.
DR   GeneTree; EBGT00050000023808; -.
DR   OMA; GALAYVD; -.
DR   ProtClustDB; PRK14022; -.
DR   BioCyc; SAUR158878:SAV1018-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cellular 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   HAMAP; MF_00208; MurE; 1; -.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; Mur_ligase_C; 1.
DR   SUPFAM; SSF53623; Mur_ligase_cen; 1.
DR   TIGRFAMs; TIGR01085; MurE; 1.
DR   HOGENOMDNA; STAAM_1.PE1011; -.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   494 AA;  UNKNOWN MW;  UNKNOWN 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 PVDQ
//

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