ID   MURF_BUCBP              Reviewed;         460 AA.
AC   Q89AQ1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE            EC=6.3.2.10;
DE   AltName: Full=UDP-MurNAc-pentapeptide synthetase;
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme;
GN   Name=murF; OrderedLocusNames=bbp_202;
OS   Buchnera aphidicola subsp. Baizongia pistaciae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=135842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; AE016826; AAO26934.1; -; Genomic_DNA.
DR   RefSeq; NP_777829.1; -.
DR   HSSP; P11880; 1GG4.
DR   GeneID; 1058402; -.
DR   GenomeReviews; AE016826_GR; bbp_202.
DR   KEGG; bab:bbp202; -.
DR   HOGENOM; Q89AQ1; -.
DR   OMA; Q89AQ1; LDDTYNA.
DR   BioCyc; BAPH224915:BBP_202-MON; -.
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-...; IEA:EC.
DR   GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-d...; 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:0007047; P: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-3pep_AlaAla_ligase.
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   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; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    460       UDP-N-acetylmuramoyl-tripeptide--D-
FT                                alanyl-D-alanine ligase.
FT                                /FTId=PRO_0000101697.
FT   NP_BIND     115    121       ATP (Potential).
SQ   SEQUENCE   460 AA;  51092 MW;  A0C2DE8052949E2C CRC64;
     MISINLIKLT SITNGILYCS NYATLHSISI HSITTDTRKI TPKCLFIALI GKNFDAHMFV
     NEAISKGAAA LLLEKQCYPK NVIPQIIVQN TTIALGKIAS WIRDQTNATV IAITGSSGKT
     SVKEMTSSIL KNCGNTISTF QNLNNNIGVP LTLLNLNKSH KYAILELGAN YPKDIEYTTK
     ITKPNIALIN NIYHSHLAGF KSLFGVAQAK QEIFLGLRKN GIAIYNKDSN YWSKWKKNLL
     TQKIINFSIK KNSTIFASNI TTSNQGSKFK IHSPNGEIYV TLPLLGYHNI SNALAAATIA
     ISINIPLEII KIGLSSLPIL KNRLQIIRLN KYKTIINDTY NANTASMIVA IKILENISGY
     KLFVAGDMLE LGKNDVLYHK IIGNTIYNSN INEVFSIGKL SKEISIASKK GHHFYNSDEL
     LKNLKNKLLN KKIITILVKA SRSEKLDVIV EQLIKEYHKA
//