ID   MURC_ANADE              Reviewed;         458 AA.
AC   Q2IG30;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_3772;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC83538.1; -; Genomic_DNA.
DR   RefSeq; YP_466975.1; -.
DR   GeneID; 3888269; -.
DR   GenomeReviews; CP000251_GR; Adeh_3772.
DR   KEGG; ade:Adeh_3772; -.
DR   HOGENOM; Q2IG30; -.
DR   OMA; Q2IG30; EWMVVEA.
DR   BioCyc; ADEH290397:ADEH_3772-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    458       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_0000242541.
FT   NP_BIND     115    121       ATP (Potential).
SQ   SEQUENCE   458 AA;  49645 MW;  0DFD0D3AC29F39AD CRC64;
     MSLFRSRQAK IHFVGVGGIG MSGIAEVLLN LGYTVSGSDL RESETTRRLA GLGGHISYGH
     AAENVLQVDV VVISSAVKRD NPEVLEARRR KIPVIPRAEM LAELMRLKYG VAIAGSHGKT
     TTTSMAAHLL AHAGLDPTAV VGGKVNAFGS NAKLGKGDYM VVEADESDGS FLRIPPTIAI
     VTNIDPEHLD HWKTPDALRR GFVDFVNRVP FYGLAILCID HPTVQSILPD VEKRVVTYGE
     SHQADYRAEA IELSGHAVRF DAFRRDEALG RFEVAMVGRH NALNALAVIA LGDEMGIPPL
     VTREALRSFQ GVQRRFTVRG EVAGVTVVDD YGHHPAEVKA TLQGAREAFK RRVVCLFQPH
     RYTRTRDLMA EFATAFNDAD VLLLTDIYAA GEEPIPGATA ANLAEAIRAW GHRDVTVVPR
     AELARAARER IRPGDLVLTL GAGDVTAAGP ELLALLER
//