(data stored in SCRATCH9089 zone)

SWISSPROT: MURC_PASMU

ID   MURC_PASMU              Reviewed;         482 AA.
AC   P57818;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=PM0143;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC         Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00046}.
DR   EMBL; AE004439; AAK02227.1; -; Genomic_DNA.
DR   RefSeq; WP_005723042.1; NC_002663.1.
DR   SMR; P57818; -.
DR   PRIDE; P57818; -.
DR   EnsemblBacteria; AAK02227; AAK02227; PM0143.
DR   KEGG; pmu:PM0143; -.
DR   PATRIC; fig|272843.6.peg.148; -.
DR   eggNOG; ENOG4105DFU; Bacteria.
DR   eggNOG; COG0773; LUCA.
DR   HOGENOM; HOG000256031; -.
DR   KO; K01924; -.
DR   OMA; DITYQLR; -.
DR   BioCyc; PMUL272843:G1FZ8-151-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00046; MurC; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01082; murC; 1.
PE   3: Inferred from homology;
DR   PRODOM; P57818.
DR   SWISS-2DPAGE; P57818.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..482
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182127"
FT   NP_BIND         131..137
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   482 AA;  52731 MW;  98667510E7A2D503 CRC64;
     MMNSKCGKAF QQRVRDMIPE MRRVRQIHFV GIGGAGMGGI AEVLLNEGYF VTGSDIMESA
     VTARLTSLGA KIAFSHAAEN IDGASVVVVS SAIRADNVEV VAAQERRIPV IQRAQMLAEI
     MRFRHGIAVA GTHGKTTTTA MISMIYAEAG LDPTFVNGGL VKSAGTNAHL GCSRYLIAEA
     DESDASFLHL QPMVSVVTNI EPDHMETYHG SFEEMKHTYV NFLHNLPFYG LAVLCADDDV
     LTELTPKVGR QVITYGFSEK ADYRIEDYQQ TGFQGHYTVI TPSGERIDVL LNVPGRHNAL
     NATAALVVAK EEGIGNEAIL AALADFQGAG RRFDQLGQFI RPNGKVMLVD DYGHHPTEVG
     VTIQAARQGW ENKRIAMIFQ PHRYSRTRDL FDDFVQVLSQ VDVLIMLDVY AAGETPIAGA
     DSRSLCRSIR NLGKVDPIFV SDHRQLGEIL DQVLQDGDLI LAQGAGNVSK IARQLAETWT
     KE
//

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