ID   MURC_BLOPB              Reviewed;         480 AA.
AC   Q493Q0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
DE            EC=6.3.2.8;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
GN   Name=murC; OrderedLocusNames=BPEN_147;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
CC   -!- FUNCTION: Cell wall formation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramate + L-alanine = ADP +
CC       phosphate + UDP-N-acetylmuramoyl-L-alanine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; CP000016; AAZ40787.1; -; Genomic_DNA.
DR   RefSeq; YP_277660.1; -.
DR   GeneID; 3562869; -.
DR   GenomeReviews; CP000016_GR; BPEN_147.
DR   KEGG; bpn:BPEN_147; -.
DR   HOGENOM; Q493Q0; -.
DR   OMA; Q493Q0; EWMVVEA.
DR   BioCyc; CBLO291272:BPEN_147-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:HAMAP.
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:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00046; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01082; murC; 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    480       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_0000242543.
FT   NP_BIND     126    132       ATP (Potential).
SQ   SEQUENCE   480 AA;  53717 MW;  F89F56671F27FCC6 CRC64;
     MSGILLSNPV NAIPLMNRIR KIHFVGIGGT GMCGIAEILA HEGYCITGSD IVYSSTTRHL
     FELGVKIFIG HKYSNINNAN VIVVSSAIHP NNPEILAAKQ ARIPVIKRAE MLSELMRFRH
     GIAISGTHGK TTTTTMIVNI YTAAGLDPTF INGGIVKSEG VHARLGYSRY LIVEADESDN
     SFLHLHPMVE VITNIDTDHI HEYQGNFEYL KKAFIDFLHN LPFYGYAIVC IDDPVICEIL
     PKIKRKIITY GFNKNANLHI FNYRQHIEKS SFTVSRFNQT KLQVTLNAPG CHNALNATAA
     IAVATEEGIS DKIILKTMLD FQGTHRRFEN LGYYSLNKIN DQTGEILLID DYGHHPAELH
     ATIVAIRTGW PDRRLVMVFQ PHRYTRIKEL YYDFIDVLSN VDILLILHVY SAGEPPILGA
     DSQSLCHAIR EFGKINPTFI SNTKMLSGAL FRLLRNNDLL LIQGAGTIGE VVRRLIVKND
//