MURU_NEIMB
ID MURU_NEIMB Reviewed; 231 AA.
AC Q9JXY0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=N-acetylmuramate alpha-1-phosphate uridylyltransferase {ECO:0000250|UniProtKB:Q88QT2};
DE Short=MurNAc-1P uridylyltransferase {ECO:0000250|UniProtKB:Q88QT2};
DE Short=MurNAc-alpha-1P uridylyltransferase {ECO:0000250|UniProtKB:Q88QT2};
DE EC=2.7.7.99 {ECO:0000250|UniProtKB:Q88QT2};
GN Name=murU {ECO:0000250|UniProtKB:Q88QT2};
GN OrderedLocusNames=NMB1841 {ECO:0000312|EMBL:AAF42176.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP FUNCTION, AND PATHWAY.
RC STRAIN=MC58;
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).
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. Is likely involved in peptidoglycan recycling as
CC part of a cell wall recycling pathway that bypasses de novo
CC biosynthesis of the peptidoglycan precursor UDP-MurNAc
CC (PubMed:23831760). Is able to complement the fosfomycin sensitivity
CC phenotype of a P.putida mutant lacking murU (PubMed:23831760).
CC {ECO:0000250|UniProtKB:Q88QT2, ECO:0000269|PubMed:23831760}.
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:0000305|PubMed:23831760}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q88QT2}.
CC -!- SIMILARITY: Belongs to the nucleotidyltransferase MurU family.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF42176.1; -; Genomic_DNA.
DR PIR; A81036; A81036.
DR RefSeq; NP_274838.1; NC_003112.2.
DR RefSeq; WP_002225669.1; NC_003112.2.
DR AlphaFoldDB; Q9JXY0; -.
DR SMR; Q9JXY0; -.
DR STRING; 122586.NMB1841; -.
DR PaxDb; Q9JXY0; -.
DR EnsemblBacteria; AAF42176; AAF42176; NMB1841.
DR KEGG; nme:NMB1841; -.
DR PATRIC; fig|122586.8.peg.2350; -.
DR HOGENOM; CLU_029499_2_1_4; -.
DR OMA; INHAHLG; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000425; 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 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 Carbohydrate metabolism; Cell shape; Cell wall biogenesis/degradation;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Peptidoglycan synthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..231
FT /note="N-acetylmuramate alpha-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000441271"
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 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
SQ SEQUENCE 231 AA; 24537 MW; D02A35622345A189 CRC64;
MKAMILAAGR GERMRPLTDT TPKPLLDVAG KPLIGWHLCR LKQAGFTEIV INHAWLGRQI
EDALGDGSAY GVNIAYSPEP AGGLETAGGI AQALPLLGGQ PFLVVNGDVL TDIDFTAAFQ
TASSLPEHIS AHLWLVENPP HNPDGDFSLL PDSSVRPEVN GGNGLTFSGV GIYRPEMFDG
IEAGSVAKLA PVLRGEMRQN RVSGQKHTGL WLDVGTVCRL KEAQALAGAW K
