MURU_PSEAE
ID MURU_PSEAE Reviewed; 224 AA.
AC Q9I5U0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=N-acetylmuramate alpha-1-phosphate uridylyltransferase {ECO:0000303|PubMed:24819062};
DE Short=MurNAc-1P uridylyltransferase {ECO:0000303|PubMed:24819062};
DE Short=MurNAc-alpha-1P uridylyltransferase {ECO:0000303|PubMed:24819062};
DE EC=2.7.7.99 {ECO:0000250|UniProtKB:Q88QT2};
GN Name=murU {ECO:0000303|PubMed:24819062};
GN OrderedLocusNames=PA0597 {ECO:0000312|EMBL:AAG03986.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24819062; DOI=10.1089/mdr.2014.0036;
RA Borisova M., Gisin J., Mayer C.;
RT "Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates
RT intrinsic resistance to fosfomycin.";
RL Microb. Drug Resist. 20:231-237(2014).
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 (By similarity). Is involved in peptidoglycan
CC recycling as part of a cell wall recycling pathway that bypasses de
CC novo biosynthesis of the peptidoglycan precursor UDP-MurNAc
CC (PubMed:24819062). Plays a role in intrinsic resistance to fosfomycin,
CC which targets the de novo synthesis of UDP-MurNAc (PubMed:24819062).
CC {ECO:0000250|UniProtKB:Q88QT2, ECO:0000269|PubMed:24819062}.
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:0000250|UniProtKB:Q88QT2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q88QT2};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:24819062}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q88QT2}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate MurNAc 1-
CC phosphate. Deletion of this gene increases fosfomycin sensitivity.
CC Growth rate is not affected. {ECO:0000269|PubMed:24819062}.
CC -!- SIMILARITY: Belongs to the nucleotidyltransferase MurU family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG03986.1; -; Genomic_DNA.
DR PIR; D83570; D83570.
DR RefSeq; NP_249288.1; NC_002516.2.
DR RefSeq; WP_003099549.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q9I5U0; -.
DR SMR; Q9I5U0; -.
DR STRING; 287.DR97_3566; -.
DR PaxDb; Q9I5U0; -.
DR PRIDE; Q9I5U0; -.
DR EnsemblBacteria; AAG03986; AAG03986; PA0597.
DR GeneID; 878173; -.
DR KEGG; pae:PA0597; -.
DR PATRIC; fig|208964.12.peg.633; -.
DR PseudoCAP; PA0597; -.
DR HOGENOM; CLU_029499_2_1_6; -.
DR InParanoid; Q9I5U0; -.
DR OMA; INHAHLG; -.
DR PhylomeDB; Q9I5U0; -.
DR BioCyc; PAER208964:G1FZ6-604-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW 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..224
FT /note="N-acetylmuramate alpha-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000441270"
FT BINDING 11..13
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 23
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
SQ SEQUENCE 224 AA; 24149 MW; 21AF1F5A2293A66D CRC64;
MKAMILAAGR GERMRPTTLH TPKPLIEAAG VPLIERQLLA LRQAGVDDWV INHAWLGEQI
EAYLGDGSRL GGRIAYSPEG EPLETGGGIF RALPLLGEQP FLLLNGDVWS DFDYSRLHLA
DGDLAHLVLV DNPAHHPAGD FHLDAGGRVG ETREAGGNLT YSGIAVLHPA LFEGCQPGAF
KLAPLLRKAI AAGRVSGEHH RGQWVDVGTH ERLAEVERLL AEHA
