MURC_FRATF
ID MURC_FRATF Reviewed; 451 AA.
AC A7N9L2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=FTA_0188;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
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}.
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DR EMBL; CP000803; ABU60665.1; -; Genomic_DNA.
DR RefSeq; WP_003014165.1; NC_009749.1.
DR AlphaFoldDB; A7N9L2; -.
DR SMR; A7N9L2; -.
DR KEGG; fta:FTA_0188; -.
DR HOGENOM; CLU_028104_2_2_6; -.
DR OMA; DITYQLR; -.
DR UniPathway; UPA00219; -.
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..451
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_1000004344"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 451 AA; 49788 MW; 7A5719518D23460B CRC64;
MNKKILFLGV GGIGVSALAI AAKRLGAHVA GYDSVANKLT AKLEALGIVI FISPNGVDVA
NFDIVVYSSA ILSSHPLLSQ ARSLGIQCLQ RAMFLAVLMK DFSYSLAITG THGKTTTSSV
LATLLCQLDK YSSFIVGGVV KYADSNIQVN GTDKLVIEAD ESDASFLFLS PQVVIITNID
LDHMATYNNS YQTLLENFTD FVSKESVKSI YLCVDDQGCR DLLAKYNQSD KNVTSYGFSI
NADVQIYDYH IIDEITHFKI RYKGDDLSFK LQLPGRYNVQ NATACIITCL DLGFKYEDIR
NALIKVTGVA RRFDLYTKVI SGHQVTVIDD YGHHPVEVAN SISAVRDRYP NKKIIHVFQP
HRYTRNRDLI KDWPKALSLA DQLILLPTYS ADEQIIKGAE SQDIVKGLSG YLLADGFDHA
IYFLEKLANE NTVILIQGAG DVTNLVEILS E