ID   MURC_BAUCH              Reviewed;         490 AA.
AC   Q1LSW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BCI_0518;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13791.1; -; Genomic_DNA.
DR   RefSeq; YP_588948.1; -.
DR   GeneID; 4056731; -.
DR   GenomeReviews; CP000238_GR; BCI_0518.
DR   KEGG; bci:BCI_0518; -.
DR   HOGENOM; Q1LSW6; -.
DR   OMA; Q1LSW6; EWMVVEA.
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    490       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_1000004312.
FT   NP_BIND     126    132       ATP (Potential).
SQ   SEQUENCE   490 AA;  54695 MW;  F3A3E80816739792 CRC64;
     MNYQRLAQLQ KLVPQMRQVK RIHFIGIGGV GMSGIAKILL HEGYQISGSD LVQNKVTKHL
     VALGVSIKFQ HIPENVLDAN VVVVSSAISI ANPEIVAAKK LRIPIITRAE MLAELMRFRY
     GIAIAGTHGK TTTTAMLASI YLEAGLDPTI VNGGLIKSIG QYARLGYGSY LIAEADESDL
     SFLHLQPIVT IITNIEADHM ENYQGDFNYL KNTFLKFIHK LPFYGKGIMC LDDPVIRDLL
     PHISRHIITY GFNSKANFRL TNYHQKEAHV SFQLYRQDKP TLRIELNSPG RHNALNAVAA
     IAVATEEGIA DKNILQALFR FKGINRRFDK LGCFSLKKIN GKNGVVMLVE DYGHHPTELQ
     ATIQSVRIGW PDKRLVMVFQ PHRYTRTRDL YEYFVGVLSK VDVLLMLDIY PAGENPIAGI
     DSKSLCCTIR NTSKLDPIFI HELNKLPVML AQLLQDNDLV LMQGAGSIGL IASQLAIGKL
     QTNIRHNPLI
//