MUPP_PSEAE
ID MUPP_PSEAE Reviewed; 226 AA.
AC Q9HZ62;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-acetylmuramic acid 6-phosphate phosphatase {ECO:0000303|PubMed:28351916};
DE Short=MurNAc 6-phosphate phosphatase {ECO:0000303|PubMed:28351916};
DE Short=MurNAc-6P phosphatase {ECO:0000303|PubMed:28351916};
DE EC=3.1.3.105 {ECO:0000250|UniProtKB:Q88M11};
GN Name=mupP {ECO:0000303|PubMed:28351916}; OrderedLocusNames=PA3172;
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 IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND MUTAGENESIS OF
RP ASP-12.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=28351916; DOI=10.1128/mbio.00102-17;
RA Fumeaux C., Bernhardt T.G.;
RT "Identification of MupP as a new peptidoglycan recycling factor and
RT antibiotic resistance determinant in Pseudomonas aeruginosa.";
RL MBio 8:0-0(2017).
CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of N-
CC acetylmuramate 6-phosphate (MurNAc-6P) to MurNac (By similarity). Is
CC involved in peptidoglycan recycling as part of a cell wall recycling
CC pathway that bypasses de novo biosynthesis of the peptidoglycan
CC precursor UDP-MurNAc (PubMed:28351916). Plays a role in intrinsic
CC resistance to fosfomycin, which targets the de novo synthesis of UDP-
CC MurNAc (PubMed:28351916). {ECO:0000250|UniProtKB:Q88M11,
CC ECO:0000269|PubMed:28351916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-muramate 6-phosphate = N-acetyl-D-muramate +
CC phosphate; Xref=Rhea:RHEA:53728, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28881, ChEBI:CHEBI:43474, ChEBI:CHEBI:58722;
CC EC=3.1.3.105; Evidence={ECO:0000250|UniProtKB:Q88M11};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q88M11};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:28351916}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene increases ampC expression
CC and promotes beta-lactam resistance similar to other peptidoglycan
CC recycling mutants. This mutant strain is hypersensitive to the
CC antibiotic fosfomycin which targets MurA activity and thus blocks the
CC conversion of UDP-GlcNAc into UDP-MurNAc as part of the de novo
CC peptidoglycan precursor synthesis pathway.
CC {ECO:0000269|PubMed:28351916}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. Phosphatase MupP subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG06560.1; -; Genomic_DNA.
DR PIR; D83249; D83249.
DR RefSeq; NP_251862.1; NC_002516.2.
DR RefSeq; WP_010895650.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; Q9HZ62; -.
DR SMR; Q9HZ62; -.
DR STRING; 287.DR97_4764; -.
DR PaxDb; Q9HZ62; -.
DR PRIDE; Q9HZ62; -.
DR DNASU; 882632; -.
DR EnsemblBacteria; AAG06560; AAG06560; PA3172.
DR GeneID; 882632; -.
DR KEGG; pae:PA3172; -.
DR PATRIC; fig|208964.12.peg.3315; -.
DR PseudoCAP; PA3172; -.
DR HOGENOM; CLU_045011_19_1_6; -.
DR InParanoid; Q9HZ62; -.
DR OMA; TPHAKPH; -.
DR PhylomeDB; Q9HZ62; -.
DR BioCyc; PAER208964:G1FZ6-3232-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IBA:GO_Central.
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:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006346; PGPase/MupP.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01449; PGP_bact; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carbohydrate metabolism; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Magnesium; Metal-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..226
FT /note="N-acetylmuramic acid 6-phosphate phosphatase"
FT /id="PRO_0000108034"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95649,
FT ECO:0000305|PubMed:28351916"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT MUTAGEN 12
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28351916"
SQ SEQUENCE 226 AA; 24977 MW; 8AE6BF83B309B92E CRC64;
MKRMRLKAVL FDMDGTLLDT APDFIAITQA MRAAHGLPPV DEQRVRDVVS GGARAMVAAA
FGLSLDSPEV EPLRQEFLDR YQEHCAVLSR PYDGIPELLA AIEKAGLIWG VVTNKPVRFA
EPIMQRLGYA ERSRVLVCPD HVTRSKPDPE PLLLACSQLG IDPSRVLFIG DDLRDIESGR
DAGTKTAAVR YGYIHPEDNP AHWGADVIVD HPRELIDVLD RALCDC
