ID   MURC_BORA1              Reviewed;         468 AA.
AC   Q2KVG1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=BAV2878;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ50488.1; -; Genomic_DNA.
DR   RefSeq; YP_787374.1; -.
DR   GeneID; 6266871; -.
DR   GenomeReviews; AM167904_GR; BAV2878.
DR   KEGG; bav:BAV2878; -.
DR   NMPDR; fig|521.1.peg.449; -.
DR   HOGENOM; Q2KVG1; -.
DR   OMA; Q2KVG1; 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    468       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_0000242544.
FT   NP_BIND     112    118       ATP (Potential).
SQ   SEQUENCE   468 AA;  49594 MW;  95FA706C1729B7E4 CRC64;
     MKHRIQHIHF VGVGGSGMSG IAEVLLNLGY TVSGSDLSES TVTRRLADLG LKVSIGHAAE
     NVADADAIVT STAVAGDNPE VIAARLARIP VVPRAVMLAE LMRLKRGIAV AGTHGKTTTT
     SLVASVLAAG GLDPTFVIGG RLNSAGANAQ LGQGEFIVVE ADESDASFLN LLPVMAIITN
     IDADHMDTYG HDVARLKSAF IEFTQRLPFY GSAVLCADDA NVREIMPFVS RPITTYGLSS
     DAQVRAENVQ ADGTRMRFSV RRQGREQDLP TLEVELNLPG LHNVRNALAA IAVASELGVA
     DAAICQALAG FKGVGRRFTQ WGEFPVAEAQ GGGRYSVIDD YGHHPVEMAA TLAAARGAWP
     DRRIVLAFQP HRYTRTRDCF EDFVRVLGTA DAVLLTEVYA AGEAPLVAAD GRALARALRV
     AGKVEPLFVE DVAALPQAVR DFMRDGDVLI LMGAGSISKV PSQLGEHA
//