MURQ_ECOLI
ID MURQ_ECOLI Reviewed; 298 AA.
AC P76535; P76965; P76966; P76967;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase;
DE Short=MurNAc-6-P etherase;
DE EC=4.2.1.126;
DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase;
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase;
GN Name=murQ; Synonyms=yfeU; OrderedLocusNames=b2428, JW2421;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=15983044; DOI=10.1074/jbc.m502208200;
RA Jaeger T., Arsic M., Mayer C.;
RT "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia
RT coli 'etherase'.";
RL J. Biol. Chem. 280:30100-30106(2005).
RN [6]
RP FUNCTION IN CELL WALL RECYCLING.
RX PubMed=16452451; DOI=10.1128/jb.188.4.1660-1662.2006;
RA Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.;
RT "MurQ etherase is required by Escherichia coli in order to metabolize
RT anhydro-N-acetylmuramic acid obtained either from the environment or from
RT its own cell wall.";
RL J. Bacteriol. 188:1660-1662(2006).
RN [7]
RP KINETIC PARAMETERS, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, AND
RP MUTAGENESIS OF GLU-83; GLU-114 AND ASP-115.
RX PubMed=18837509; DOI=10.1021/bi8014532;
RA Hadi T., Dahl U., Mayer C., Tanner M.E.;
RT "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ):
RT an etherase involved in peptidoglycan recycling.";
RL Biochemistry 47:11547-11558(2008).
RN [8]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18723630; DOI=10.1128/jb.00642-08;
RA Jaeger T., Mayer C.;
RT "The transcriptional factors MurR and catabolite activator protein regulate
RT N-acetylmuramic acid catabolism in Escherichia coli.";
RL J. Bacteriol. 190:6598-6608(2008).
CC -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether
CC substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-
CC lactate. Is required for growth on MurNAc as the sole source of carbon
CC and energy. Together with AnmK, is also required for the utilization of
CC anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the
CC medium or derived from its own cell wall murein, and thus plays a role
CC in cell wall recycling. {ECO:0000269|PubMed:15983044,
CC ECO:0000269|PubMed:16452451}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-
CC acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:26410,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16004, ChEBI:CHEBI:57513,
CC ChEBI:CHEBI:58722; EC=4.2.1.126;
CC Evidence={ECO:0000269|PubMed:15983044};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.20 mM for N-acetylmuramic acid 6-phosphate
CC {ECO:0000269|PubMed:18837509};
CC Note=kcat is 5.7 sec(-1).;
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18837509}.
CC -!- INDUCTION: Induced by MurNAc 6-phosphate that releases the repressor
CC MurR from the DNA. Also up-regulated by the cAMP receptor protein crp
CC via the binding of crp-cAMP to a class I site upstream of the murQ
CC promoter. Repressed by MurR in the absence of MurNAc 6-phosphate.
CC {ECO:0000269|PubMed:18723630}.
CC -!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is
CC suggested for the cleavage of the lactyl ether bond of MurNAc 6-
CC phosphate, with the formation of an alpha,beta-unsaturated aldehyde
CC intermediate with (E)-stereochemistry, followed by the syn addition of
CC water to give product.
CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC75481.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16312.2; -; Genomic_DNA.
DR PIR; C65017; C65017.
DR RefSeq; NP_416923.1; NC_000913.3.
DR RefSeq; WP_001159160.1; NZ_LN832404.1.
DR AlphaFoldDB; P76535; -.
DR SMR; P76535; -.
DR BioGRID; 4260569; 7.
DR IntAct; P76535; 6.
DR STRING; 511145.b2428; -.
DR jPOST; P76535; -.
DR PaxDb; P76535; -.
DR PRIDE; P76535; -.
DR EnsemblBacteria; AAC75481; AAC75481; b2428.
DR EnsemblBacteria; BAA16312; BAA16312; BAA16312.
DR GeneID; 946893; -.
DR KEGG; ecj:JW2421; -.
DR KEGG; eco:b2428; -.
DR PATRIC; fig|1411691.4.peg.4303; -.
DR EchoBASE; EB3914; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_6; -.
DR InParanoid; P76535; -.
DR OMA; CPPTFCT; -.
DR PhylomeDB; P76535; -.
DR BioCyc; EcoCyc:G7263-MON; -.
DR BioCyc; MetaCyc:G7263-MON; -.
DR UniPathway; UPA00342; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR PRO; PR:P76535; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IDA:EcoCyc.
DR GO; GO:0016803; F:ether hydrolase activity; IDA:EcoliWiki.
DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046348; P:amino sugar catabolic process; IMP:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009254; P:peptidoglycan turnover; IMP:EcoCyc.
DR CDD; cd05007; SIS_Etherase; 1.
DR HAMAP; MF_00068; MurQ; 1.
DR InterPro; IPR005488; Etherase_MurQ.
DR InterPro; IPR005486; Glucokinase_regulatory_CS.
DR InterPro; IPR040190; MURQ/GCKR.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10088; PTHR10088; 1.
DR PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00274; TIGR00274; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Reference proteome.
FT CHAIN 1..298
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000214829"
FT DOMAIN 55..218
FT /note="SIS"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:18837509"
FT ACT_SITE 114
FT /evidence="ECO:0000305|PubMed:18837509"
FT MUTAGEN 83
FT /note="E->A: 10000-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18837509"
FT MUTAGEN 83
FT /note="E->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18837509"
FT MUTAGEN 114
FT /note="E->Q: 2000-fold reduction in catalytic activity and
FT 4-fold increase in substrate affinity."
FT /evidence="ECO:0000269|PubMed:18837509"
FT MUTAGEN 115
FT /note="D->N: 7-fold reduction in catalytic activity and
FT 1.5-fold increase in substrate affinity."
FT /evidence="ECO:0000269|PubMed:18837509"
SQ SEQUENCE 298 AA; 31220 MW; 34FE8F878E8B3077 CRC64;
MQFEKMITEG SNTASAEIDR VSTLEMCRII NDEDKTVPLA VERVLPDIAA AIDVIHAQVS
GGGRLIYLGA GTSGRLGILD ASECPPTYGV KPGLVVGLIA GGEYAIQHAV EGAEDSREGG
VNDLKNINLT AQDVVVGIAA SGRTPYVIAG LEYARQLGCR TVGISCNPGS AVSTTAEFAI
TPIVGAEVVT GSSRMKAGTA QKLVLNMLST GLMIKSGKVF GNLMVDVVAT NEKLHVRQVN
IVKNATGCSA EQAEAALIAC ERNCKTAIVM VLKNLDAAEA KKRLDQHGGF IRQVLDKE
