ID   MURC_BORAP              Reviewed;         468 AA.
AC   Q0SM34;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=BAPKO_0870;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH02094.1; -; Genomic_DNA.
DR   RefSeq; YP_710270.1; -.
DR   GeneID; 4227147; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0870.
DR   KEGG; baf:BAPKO_0870; -.
DR   NMPDR; fig|390236.5.peg.872; -.
DR   HOGENOM; Q0SM34; -.
DR   OMA; Q0SM34; EWMVVEA.
DR   BioCyc; BAFZ390236:BAPKO_0870-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    468       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_0000336817.
FT   NP_BIND     121    127       ATP (Potential).
SQ   SEQUENCE   468 AA;  53553 MW;  04DCD1F0449B9669 CRC64;
     MKVDFDSLNN IFFVGIKGSG VCSLACFLNS KGYFVEGVDV SDKFHTDKIL SNNKISYYEN
     IYEFSLKELG RSFDLIVYSS AYDKYGLPAL LEAKELNIPI LSYSEVLGEL SRKYYSVGIA
     GSHGKTTTTA FLGLLFNKLG LNPNVIVGSS VKDFGDNSAI AGISNIFIAE TCEYKKHFLH
     FSPNMLILTN IDYEHVDFFE NYEALEDAFL QYINNLKKNG ILIINSDDNN LLKIKRQINR
     KDINIFSFGS KDLSNFQISN IVVKNEYFCF SFLGLCNVEL RTVLFHNVLN FSAALLALNL
     FLESNGKSIF DFEEAVKKIA KNYSGIKRRV EVVKEKKGVI YMDDYAHHPR EIRDTLLGIK
     DFYKNKRIIL DFMPHTFTRT KEFFNDFVEV LSVADILILH NIYLSNRENF NPDELSVKLF
     LNIKKINKNT YFFKDVKDSV EFIKSLLISG DLFITMGAGN NFILHDFL
//