ID   MURC_BUCAP              Reviewed;         483 AA.
AC   O51926;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=BUsg_209;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9425245; DOI=10.1007/s002849900284;
RA   Baumann L., Baumann P.;
RT   "Characterization of ftsZ, the cell division gene of Buchnera aphidicola
RT   (endosymbiont of aphids) and detection of the product.";
RL   Curr. Microbiol. 36:85-89(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Baumann L., Baumann P.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [4]
RP   TRANSCRIPTIONAL SLIPPAGE.
RX   PubMed=18815381; DOI=10.1073/pnas.0806554105;
RA   Tamas I., Wernegreen J.J., Nystedt B., Kauppinen S.N., Darby A.C.,
RA   Gomez-Valero L., Lundin D., Poole A.M., Andersson S.G.;
RT   "Endosymbiont gene functions impaired and rescued by polymerase infidelity
RT   at poly(A) tracts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14934-14939(2008).
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}.
CC   -!- CAUTION: The gene is frameshifted. However, transcriptional slippage at
CC       poly(A) may correct the reading frame, which can potentially yield
CC       full-length protein. {ECO:0000305|PubMed:18815381}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC46066.2; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AE013218; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF012886; AAC46066.2; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE013218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; O51926; -.
DR   SMR; O51926; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000416; 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;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..483
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182069"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
FT   CONFLICT        131..133
FT                   /note="TTS -> LLA (in Ref. 1; AAC46066)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  54844 MW;  E3C3E4986667EC10 CRC64;
     MNINKIKKNN FFKEKKILKI HLIGIAGSGM SGIALILFNL GYKISGSDLL ENFMTKKLKN
     MGINIYFQHS EENIKYADFI IISSAIPSDN PEIKAAKKKN IPILLRAEML QIFMQFKFGI
     AVSGTHGKTT TTSMIFDILN QNKLDPTVIN GGLIKSINSH AKLGFSKYFI AEADESDGSF
     LCLNPTTAII TNIEPDHIDN YNGEFKLLKK TFLDFLNKIP SYGIAILCTD NKAILNILPK
     IKCKVITYGF NKSAEFRITS YKQSDFISNF TLIRKKQLNN LEIILNLPGE HNALNATAAI
     AFATYQKIPD EKIYQSLKNF KGTSRRFEYV GKLFIKKKSI QNKSVMLIND YGHHPTELSE
     TIKTIRKSWP KKNLIMIFQP HRYTRTRNLY FDFIKILSQV DSLLILNVYS ANESFISGAD
     SFSLYSDIKK IKKNVILVTN RNLILNYLLP HLNGNDIILI QGAGDIDTII NKIFILKNKK
     VII