ID   MURC_ALCBS              Reviewed;         474 AA.
AC   Q0VS01;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=ABO_0599;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL16047.1; -; Genomic_DNA.
DR   RefSeq; YP_692319.1; -.
DR   GeneID; 4211241; -.
DR   GenomeReviews; AM286690_GR; ABO_0599.
DR   KEGG; abo:ABO_0599; -.
DR   NMPDR; fig|393595.12.peg.597; -.
DR   HOGENOM; Q0VS01; -.
DR   OMA; Q0VS01; EWMVVEA.
DR   BioCyc; ABOR393595:ABO_0599-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    474       UDP-N-acetylmuramate--L-alanine ligase.
FT                                /FTId=PRO_1000004306.
FT   NP_BIND     123    129       ATP (Potential).
SQ   SEQUENCE   474 AA;  51161 MW;  D4EDC6BF5E857C73 CRC64;
     MADNDIIHTV PEMRRIRGIH FVGIGGVGMC GIAEVLANQG YAISGSDIKE SPVLERLRSL
     GVRVDIGHRA ENIDGADVVV TSTAVNTENL EVAAAHERRI PVVPRAQMLA ELMRFRHGIA
     VAGTHGKTTT TSLTAAIMAE AGLDPTFVIG GRLNSAGTNA RLGQSRYLVA EADESDASFL
     HLQPMSAIVT NVDADHMHTY GGDFAQLENT FIEFLHNLPF YGVAVMCVDD PVVRKLLPRV
     NRQVIRYGFS EDADLRAENV RQDGMVTHFR VVRAEGEPLD VSLNMPGRHN VLNALAAIAV
     SADEGAGDEA IIRGLNNFTG VGRRFDVQGD YHFDGGSATL VDDYGHHPRE VAATIDAIRE
     GWPGRRLAML FQPHRYTRTQ DLYEDFVEVL SGVDVLLMLE VYAAGEEPIP GADARALCRS
     LRKRGLEPVF VDDPDKLQGL LASQLQNGDL LVTQGAGNVG AIAKQLVAQG GGHG
//