ID   MURC_ANAVT              Reviewed;         494 AA.
AC   Q3MAP8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Ava_2320;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
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., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA21938.1; -; Genomic_DNA.
DR   RefSeq; YP_322833.1; -.
DR   GeneID; 3683590; -.
DR   GenomeReviews; CP000117_GR; Ava_2320.
DR   KEGG; ava:Ava_2320; -.
DR   NMPDR; fig|240292.3.peg.199; -.
DR   HOGENOM; Q3MAP8; -.
DR   OMA; Q3MAP8; EWMVVEA.
DR   BioCyc; AVAR240292:AVA_2320-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    494       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_0000242540.
FT   NP_BIND     140    146       ATP (Potential).
SQ   SEQUENCE   494 AA;  53541 MW;  52A6CC110CB43639 CRC64;
     MNNSVDFGGR PFHFIGIGGI GMSALAYVLA KRQLPVSGSD LRPNHITRKL ESIGAHIFSR
     QEASNLEFFG SKVSSTEIEL NTQEMFPLGK STLPQVVCST AINSNNLEYQ AAIELGCPIL
     HRSDVLAALI NDYHSVAVAG THGKTTTSSM IGYMLLEAGL DPTIIVGGEV NAWEGNARLG
     QSPYLVAEAD ESDGSLVKHA PEIGIITNIE LDHPDHYDTL EEVVDIFQTF AKGCKTLIGS
     VDCATVRELL RTAASDRQQP TITYSLHQDT EADYTVTNID CRADGTTALV WEKGKALGVL
     KLKLLSRHNL SNALAAVAVG RLVGLEFGEI AKGIAGFEGA RRRFEFRGEV DGITFIDDYA
     HHPSEIRATL AAARLQARPG QRVVAIFQPH RYSRTLTFLE EFSESFSHAD LVVLTDIYSA
     GEPNLGLISG EQLAEKIAQE HPQVVYQPTL STVCEYLLKN LRPGDLALFL GAGNLNQAIP
     EIITTLCEPA TATL
//