MURU_CAUVC
ID MURU_CAUVC Reviewed; 242 AA.
AC Q9A2M1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CC_3536 {ECO:0000312|EMBL:AAK25498.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 19089 / CB15;
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; AE005673; AAK25498.1; -; Genomic_DNA.
DR PIR; F87687; F87687.
DR RefSeq; NP_422330.1; NC_002696.2.
DR RefSeq; WP_010921365.1; NC_002696.2.
DR AlphaFoldDB; Q9A2M1; -.
DR SMR; Q9A2M1; -.
DR STRING; 190650.CC_3536; -.
DR EnsemblBacteria; AAK25498; AAK25498; CC_3536.
DR KEGG; ccr:CC_3536; -.
DR PATRIC; fig|190650.5.peg.3542; -.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_029499_2_1_5; -.
DR OMA; INHAHLG; -.
DR BioCyc; CAULO:CC3536-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001816; 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; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF12804; NTP_transf_3; 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..242
FT /note="N-acetylmuramate alpha-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000441272"
FT BINDING 16..18
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 28
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q88QT2"
SQ SEQUENCE 242 AA; 25590 MW; 90361B198B57B8CF CRC64;
MSQAPKIAMV LAAGLGTRMR PLTNDRPKAL VEVAGKALID HMLDRLVAAS VETAVVNVHY
FADLVEAHLR AREAKGLAPR IVISDERVQA LETGGGIKHA LALLGEGPVF VANIDSIWIE
HAGAAVDAVA AAWDPERMDV CLMLASTTES LGFHDTGDVF LSADGLVRFK DAGEIAPLVY
VGVHICKPEI TADGPDGPFS LLPLWKRLAA DGRVCGVAPE GLWMHVGDPQ AKLAAEARLA
EA
