(data stored in ACNUC7421 zone)

HOGENOM: LEGP2_1_PE1002

ID   LEGP2_1_PE1002                       STANDARD;      PRT;   483 AA.
AC   LEGP2_1_PE1002; D5TB63;
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   SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2,
DE   6-diaminopimelate ligase; EC=6.3.2 13; (LEGP2_1.PE1002).
GN   Name=murE; OrderedLocusNames=lpa_01386;
OS   LEGIONELLA PNEUMOPHILA 2300/99 ALCOY.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=423212;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEGP2_1.PE1002.
CC       Legionella pneumophila 2300/99 Alcoy chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D5TB63_LEGP2
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
CC   -!- GENE_FAMILY: HOG000268118 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D5TB63; -.
DR   EMBL; CP001828; ADG24247.1; -; Genomic_DNA.
DR   RefSeq; YP_003618199.1; NC_014125.1.
DR   ProteinModelPortal; D5TB63; -.
DR   GeneID; 9128776; -.
DR   GenomeReviews; CP001828_GR; lpa_01386.
DR   KEGG; lpa:lpa_01386; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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:HAMAP.
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; LEGP2_1.PE1002; -.
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   483 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKLTQLLEPW IKRDIIDGTV SDIKNDSRLV KEGDLFVAYP GAASDGRLYI EKAVASGAVA
     VVYEPNNLPQ GITLPTAIPC IAIPQLAEKL GEIAKRFFNN PSQFLGLTGV TGTNGKTTIA
     YQLAQAHDLL GQHSAYIGTI GQGKVDALKP LENTTPDALC LQRLMHQYKE EGIKQVCMEV
     SSHALSQHRV DSLEFSQAIF TNLTLDHLDY HQTMQAYGAA KSRLFERAEL QWAIINQDDD
     FQDLMSNVLK THVKKVTYGM HQNCDVKALQ WNMDITGTEI EVKSPWGHQL LKIKALGKFN
     IYNSLAVYSS LLASGHNPEK VVQVMAELKA APGRMEIVAQ SPYVLVDYAH TPDALENVLI
     TLKQIKKGRL WVVFGCGGDR DKTKRPIMGK AASMYADNIV ITSDNPRSED PEIILNEIAC
     GIPASAPVSK LVNREEAIAY ALRKAEHNDI ILIAGKGHES YQQIGNTKHV FSDQEVVRRL
     MNN
//

If you have problems or comments...

PBIL Back to PBIL home page