ID G0BNY9_9ENTR Unreviewed; 453 AA.
AC G0BNY9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 03-APR-2013, entry version 15.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE EC=6.3.2.10;
GN ORFNames=SerAS12_0691;
OS Serratia sp. AS12.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Serratia.
OX NCBI_TaxID=768490;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AS12;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Neupane S., Alstrom S.,
RA Finlay R., Hogberg N., Woyke T.;
RT "Complete sequence of Serratia sp. AS12.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; CP002774; AEF48798.1; -; Genomic_DNA.
DR RefSeq; YP_004499155.1; NC_015566.1.
DR EnsemblBacteria; AEF48798; AEF48798; SerAS12_0691.
DR GeneID; 10624883; -.
DR KEGG; srs:SerAS12_0691; -.
DR KO; K01929; -.
DR UniPathway; UPA00219; -.
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; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 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 PANTHER; PTHR23135:SF3; PTHR23135:SF3; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis.
SQ SEQUENCE 453 AA; 47349 MW; 73259A8660255CBE CRC64;
MIPVSLQALA DVLSAELIGA DCQIIEVTTD TRQVTAGCLF VALKGERFDA HAFAADAVAA
GAGALLVSKR LLVDVPQLVV KDTRLALGQL AAWVRQQVPA RVVALTGSSG KTSVKEMVAA
ILRECGEVLY TAGNFNNDIG VPLTLLRLQP QHDFAVIELG ANHIGEIAYT TALTRPQTAL
VNNLAAAHLE GFGSLAGVAQ AKGEIFTGLP ADGVAIINAD NNDWPHWQSM LNGKTVWRFS
PQAAEGVDFF ASDVLVNAKG TQFTLHSPFG TAVVTLPLPG RHNVANALAA AALAMSVGAS
LESVRQGLKQ LQGVPGRLFP IALTENKLLL DDSYNANVGS MTAAAQVLAE MPGYRVMVVG
DMAELGADAE ECHRQVGEAA RLAGIDKVIG IGPLSQALCA ASGNGEHFQN KAAVIARVAE
LLSEHAVITV LIKGSRSAAM EQVVRALQEK APC
//
