ID   MURC_BURCM              Reviewed;         465 AA.
AC   Q0BIK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Bamb_0464;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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; CP000440; ABI86023.1; -; Genomic_DNA.
DR   RefSeq; YP_772357.1; -.
DR   GeneID; 4311153; -.
DR   GenomeReviews; CP000440_GR; Bamb_0464.
DR   KEGG; bam:Bamb_0464; -.
DR   NMPDR; fig|339670.3.peg.6101; -.
DR   OMA; Q0BIK0; 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    465       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_1000004319.
FT   NP_BIND     112    118       ATP (Potential).
SQ   SEQUENCE   465 AA;  48979 MW;  9F5985295DCC78E6 CRC64;
     MKHIVKQIHF VGIGGAGMSG IAEVLVNLGY EVSGSDLSRN AVTDRLEALG ARIAIGHDAA
     NIAGANAVVV STAVRSDNPE VLAARHQGVP IVQRAVMLAE LMRLKQGIAI AGTHGKTTTT
     SLVASVLAAG GLDPTFVIGG RLISAGANAR LGTGDFIVAE ADESDASFLN LYPVIEVITN
     IDADHMDTYG HDFARLKQAF IEFTQRLPFY GSAVVCVDDP NVRQIIPFIS KPVVRYGLSP
     DAQVRAEDID ARDGRMHFTV IREGRAPLAV VLNLPGLHNV QNALAAIAIA TDLGVSDDAI
     QQALAEFNGV GRRFQRYGEV PSADGGQYTL IDDYGHHPVE MAATVAAARG AFPGRRLVLA
     FQPHRYTRTR DCFDDFVNVL STVDALVLTE VYAAGEAAIT TANGDALSRA LRAVGRVDPV
     FVASVDDVPD ALAGVARNGD VVITMGAGSI GGVPAKIVQH IQQKA
//