(data stored in ACNUC7421 zone)

HOGENOM: ESCOL4_1_PE100

ID   ESCOL4_1_PE100                       STANDARD;      PRT;   452 AA.
AC   ESCOL4_1_PE100; Q8FL66;
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-tripeptide--D-alanyl-D-alanine ligase;
DE   EC=6.3.2 10; (ESCOL4_1.PE100).
GN   Name=murF; OrderedLocusNames=c0104;
OS   ESCHERICHIA COLI CFT073.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL4_1.PE100.
CC       Escherichia coli CFT073, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q8FL66_ECOL6
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final
CC       step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
CC       precursor of murein (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-
CC       glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-
CC       acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC       alanine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
CC   -!- GENE_FAMILY: HOG000268120 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8FL66; -.
DR   EMBL; AE014075; AAN78602.1; -; Genomic_DNA.
DR   RefSeq; NP_752058.1; NC_004431.1.
DR   HSSP; P11880; 1GG4.
DR   ProteinModelPortal; Q8FL66; -.
DR   SMR; Q8FL66; 1-447.
DR   EnsemblBacteria; EBESCT00000045144; EBESCP00000043493; EBESCG00000044194.
DR   GeneID; 1035941; -.
DR   GenomeReviews; AE014075_GR; c0104.
DR   KEGG; ecc:c0104; -.
DR   NMPDR; fig|199310.1.peg.102; -.
DR   GeneTree; EBGT00050000009467; -.
DR   OMA; YAVIEMG; -.
DR   ProtClustDB; PRK10773; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:EC.
DR   GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEADR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005863; UDP-N-AcMur-pentapeptide_synth.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   PANTHER; PTHR23135:SF3; MurF; 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; TIGR01143; MurF; 1.
DR   HOGENOMDNA; ESCOL4_1.PE100; -.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Ligase;
KW   Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   452 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MISVTLSQLT DILNGELQGA DITLDAVTTD TRKLTPGCLF VALKGERFDA HDFADQAKAG
     GAGALLVSRP LDIDLPQLIV KDTRLAFGEL AAWVRQQVPA RVVALTGSSG KTSVKEMTAA
     ILSQCGNTLY TAGNLNNDIG VPMTLLRLTP EYDYAVIELG ANHQGEIAWT VSLTRPEAAL
     VNNLAAAHLE GFGSLAGVAK AKGEIFSGLP ENGIAIMNAD NNDWLNWQSV IGSRKVWRFS
     PNAANSDFTA TNIHVTSHGT EFTLQTPTGS VDVLLPLPGC HNIANALAAA ALSMSVGATL
     DAIKAGLANL KAVPGRLFPI KLAENQLLLD DSYNANVGSM TAAVQVLAEM PGYRVLVVGD
     MAELGAESEA CHVQVGEAAK AAGIDRVLSV GKQSHAISTA SGVGEHFSDK TALIARLKSL
     IAEQQVITIL VKGSRSAAME EVVRALQENG TC
//

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