ID B8FPP4_DESHD Unreviewed; 453 AA.
AC B8FPP4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 29-MAY-2013, entry version 37.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE EC=6.3.2.10;
GN OrderedLocusNames=Dhaf_1662;
OS Desulfitobacterium hafniense (strain DCB-2 / DSM 10664).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCB-2 / DSM 10664;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Madsen T., Christiansen N., Ahring B.,
RA Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.;
RT "Complete sequence of Desulfitobacterium hafniense DCB-2.";
RL Submitted (DEC-2008) 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; CP001336; ACL19708.1; -; Genomic_DNA.
DR RefSeq; YP_002458144.1; NC_011830.1.
DR ProteinModelPortal; B8FPP4; -.
DR STRING; 272564.Dhaf_1662; -.
DR EnsemblBacteria; ACL19708; ACL19708; Dhaf_1662.
DR GeneID; 7258631; -.
DR KEGG; dhd:Dhaf_1662; -.
DR PATRIC; 21661059; VBIDesHaf15223_1732.
DR eggNOG; COG0770; -.
DR HOGENOM; HOG000268120; -.
DR KO; K01929; -.
DR OMA; HIGQLKT; -.
DR ProtClustDB; CLSK2466776; -.
DR BioCyc; DHAF272564:GCV8-1687-MONOMER; -.
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; Complete proteome; Ligase;
KW Nucleotide-binding; Peptidoglycan synthesis.
SQ SEQUENCE 453 AA; 48672 MW; 0EFD49C323DA5C2E CRC64;
MEMTVREIVA ACGGKLLCGD PDTMVTSVVT DSRKVTDGSL FVPLKGEKAD AHTFLHAAFA
SGAAAALTQE HMRMEAEEAW IAVDSTQLAL QQIAAAYRQR FSIPVVGITG SAGKTTTKEM
TALALSAGYK VMKTGGNHNS QIGLPLMMFQ FSWEHEAAVV EMGISDFGEM ARLAQVAEPK
YAVMTNLGIT HIGQLKTQGN ILREKLHITD RFTQGSVLFL NGDDPMLAGL RGKTGYETVF
YGRLPWCDFR AEGITVQEET TAFRCLAPGS ESVEVTLPVL GMHHVLDALA ALAVAERLGV
PLKRAAAALR DYRPLAMRQQ IYHVNEVAVI DDSYNSSPGA AKSSLSVLAG FRAGRRVAVL
ADMLELGEYS RQAHFEVGVC AAENGVDILL TVGQEAKAVA EGARSVRAGI DCRVLDNNYQ
AAEELKSFLS PGDAVLVKGS RGMHTEEIVR ALL
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