MURC_PORGI
ID MURC_PORGI Reviewed; 456 AA.
AC Q51831;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 150.
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=PG_0581;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=381;
RX PubMed=7496515; DOI=10.1099/13500872-141-9-2047;
RA Ansai T., Yamashita Y., Awano S., Shibata Y., Wachi M., Nagai K.,
RA Takehara T.;
RT "A murC gene in Porphyromonas gingivalis 381.";
RL Microbiology 141:2047-2052(1995).
RN [2]
RP SEQUENCE REVISION.
RA Ansai T.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {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; D84504; BAA24358.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65768.1; -; Genomic_DNA.
DR RefSeq; WP_005873943.1; NC_002950.2.
DR AlphaFoldDB; Q51831; -.
DR SMR; Q51831; -.
DR STRING; 242619.PG_0581; -.
DR EnsemblBacteria; AAQ65768; AAQ65768; PG_0581.
DR KEGG; pgi:PG_0581; -.
DR PATRIC; fig|242619.8.peg.530; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_10; -.
DR OMA; DITYQLR; -.
DR OrthoDB; 307881at2; -.
DR BioCyc; PGIN242619:G1G02-539-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000588; 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; Reference proteome.
FT CHAIN 1..456
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182134"
FT BINDING 114..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 241
FT /note="Q -> R (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="G -> E (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="H -> R (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="R -> K (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="E -> Q (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..456
FT /note="Missing (in Ref. 1; BAA24358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50744 MW; AFE9DEAE93D85D91 CRC64;
MKRVYFIGIG GIGMSAIARY FHAKGFNVCG YDLTPSPITD QLIKEGIEVH FSDDLNMIPK
AFFSPTDSLI VYTPAVPADH SELTYFRSNG YRVVKRAEVL GEITLMERAL CVAGTHGKTT
TSTLLAHLLK QSHVDCNAFL GGISNNYQSN LLLSDKSDLV VVEADEFDRS FHHLKPFMAI
ITSADPDHMD IYGTAENYRD SFEHFTSLIQ SGGALVLKYG APVNPRLGSD VSLFTYSSDD
QQADYFASDI MIRDGRLFFT WHYPGGQLEG VELGVPVRIN VENAVAAMAI AHLNGVTVEE
LRSGIASFKG SHRRFEKVLD TERVVLIDDY AHHPVELDAA IHSVREIYSG KHIMGIFQPH
LYSRTADFYQ DFARSLSMLD EVVLLDIYPA RELPLPGVTS RLILDLIENP NKTLVSKNDL
LDYLHGNEIP DVVLILGAGD IDRLVIPVKQ YLQTLC
