MURU_PSEPK
ID MURU_PSEPK Reviewed; 223 AA.
AC Q88QT2; A0A0J9X280;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=N-acetylmuramate alpha-1-phosphate uridylyltransferase {ECO:0000303|PubMed:23831760};
DE Short=MurNAc-1P uridylyltransferase {ECO:0000303|PubMed:23831760};
DE Short=MurNAc-alpha-1P uridylyltransferase {ECO:0000303|PubMed:23831760};
DE EC=2.7.7.99 {ECO:0000269|PubMed:23831760, ECO:0000269|PubMed:25767118};
GN Name=murU {ECO:0000303|PubMed:23831760};
GN OrderedLocusNames=PP_0406 {ECO:0000312|EMBL:AAN66036.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND PATHWAY.
RX PubMed=23831760; DOI=10.1038/nchembio.1289;
RA Gisin J., Schneider A., Naegele B., Borisova M., Mayer C.;
RT "A cell wall recycling shortcut that bypasses peptidoglycan de novo
RT biosynthesis.";
RL Nat. Chem. Biol. 9:491-493(2013).
RN [3] {ECO:0007744|PDB:4Y7T, ECO:0007744|PDB:4Y7U, ECO:0007744|PDB:4Y7V}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF NATIVE ENZYME AND IN COMPLEXES
RP WITH MURNAC-ALPHA1-P; UTP ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=25767118; DOI=10.1074/jbc.m114.620989;
RA Renner-Schneck M., Hinderberger I., Gisin J., Exner T., Mayer C.,
RA Stehle T.;
RT "Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-
RT alpha1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase
RT and potential drug target enzyme in Gram-negative pathogens.";
RL J. Biol. Chem. 290:10804-10813(2015).
CC -!- FUNCTION: Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc),
CC a crucial precursor of the bacterial peptidoglycan cell wall, from UTP
CC and MurNAc-alpha-1P (PubMed:23831760, PubMed:25767118). Is involved in
CC peptidoglycan recycling as part of a cell wall recycling pathway that
CC bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc
CC (PubMed:23831760). Plays a role in intrinsic resistance to fosfomycin,
CC which targets the de novo synthesis of UDP-MurNAc (PubMed:23831760). Is
CC not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates
CC (PubMed:23831760). Cannot accept other nucleotide triphosphates (ATP,
CC CTP, TTP, or GTP) than UTP (PubMed:25767118).
CC {ECO:0000269|PubMed:23831760, ECO:0000269|PubMed:25767118}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-muramate 1-phosphate + UDP = phosphate
CC + UDP-N-acetyl-alpha-D-muramate; Xref=Rhea:RHEA:53716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:70757, ChEBI:CHEBI:137594; EC=2.7.7.99;
CC Evidence={ECO:0000269|PubMed:23831760, ECO:0000269|PubMed:25767118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25767118};
CC -!- ACTIVITY REGULATION: Is completely inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:25767118}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:23831760}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25767118}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate MurNAc
CC phosphate. Deletion of this gene increases fosfomycin sensitivity.
CC {ECO:0000269|PubMed:23831760}.
CC -!- SIMILARITY: Belongs to the nucleotidyltransferase MurU family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN66036.1; -; Genomic_DNA.
DR RefSeq; NP_742572.1; NC_002947.4.
DR RefSeq; WP_010951745.1; NC_002947.4.
DR PDB; 4Y7T; X-ray; 1.80 A; A=1-223.
DR PDB; 4Y7U; X-ray; 1.70 A; A=1-223.
DR PDB; 4Y7V; X-ray; 1.80 A; A=1-223.
DR PDBsum; 4Y7T; -.
DR PDBsum; 4Y7U; -.
DR PDBsum; 4Y7V; -.
DR AlphaFoldDB; Q88QT2; -.
DR SMR; Q88QT2; -.
DR STRING; 160488.PP_0406; -.
DR EnsemblBacteria; AAN66036; AAN66036; PP_0406.
DR KEGG; ppu:PP_0406; -.
DR PATRIC; fig|160488.4.peg.438; -.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_029499_2_1_6; -.
DR OMA; INHAHLG; -.
DR PhylomeDB; Q88QT2; -.
DR BioCyc; MetaCyc:G1G01-443-MON; -.
DR BioCyc; PPUT160488:G1G01-443-MON; -.
DR BRENDA; 2.7.7.99; 5092.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0070569; F:uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002134; F:UTP binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0097172; P:N-acetylmuramic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Carbohydrate metabolism; Cell shape;
KW Cell wall biogenesis/degradation; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..223
FT /note="N-acetylmuramate alpha-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000441269"
FT BINDING 11..13
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:25767118,
FT ECO:0007744|PDB:4Y7U"
FT BINDING 23
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:25767118,
FT ECO:0007744|PDB:4Y7U"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25767118,
FT ECO:0007744|PDB:4Y7U, ECO:0007744|PDB:4Y7V"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25767118"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25767118,
FT ECO:0007744|PDB:4Y7U, ECO:0007744|PDB:4Y7V"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25767118"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25767118,
FT ECO:0007744|PDB:4Y7U, ECO:0007744|PDB:4Y7V"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4Y7U"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4Y7U"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:4Y7U"
SQ SEQUENCE 223 AA; 23814 MW; 1F69642E3BE4DD5E CRC64;
MKAMILAAGK GERMRPLTLH TPKPLVPVAG QPLIEYHLRA LAAAGVTEVV INHAWLGQQI
EDHLGDGSRF GLSIRYSPEG EPLETGGGIF KALPLLGDAP FLLVNGDVWT DYDFARLQAP
LQGLAHLVLV DNPGHHGRGD FRLVGEQVVD GDDAPGTLTF SGISVLHPAL FEGCQAGAFK
LAPLLRQAMA AGKVSGEHYR GHWVDVGTLE RLAEAESLIG ERA
