MUPP_PSEPK
ID MUPP_PSEPK Reviewed; 223 AA.
AC Q88M11;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=N-acetylmuramic acid 6-phosphate phosphatase {ECO:0000303|PubMed:28351914};
DE Short=MurNAc 6-phosphate phosphatase {ECO:0000303|PubMed:28351914};
DE Short=MurNAc-6P phosphatase {ECO:0000303|PubMed:28351914};
DE EC=3.1.3.105 {ECO:0000269|PubMed:28351914};
GN Name=mupP {ECO:0000303|PubMed:28351914};
GN Synonyms=gph {ECO:0000312|EMBL:AAN67384.1};
GN OrderedLocusNames=PP_1764 {ECO:0000312|EMBL:AAN67384.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=28351914; DOI=10.1128/mbio.00092-17;
RA Borisova M., Gisin J., Mayer C.;
RT "The N-Acetylmuramic acid 6-phosphate phosphatase MupP completes the
RT Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin
RT resistance.";
RL MBio 8:0-0(2017).
CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of N-
CC acetylmuramate 6-phosphate (MurNAc-6P) to MurNac. Is involved in
CC peptidoglycan recycling as part of a cell wall recycling pathway that
CC bypasses de novo biosynthesis of the peptidoglycan precursor UDP-
CC MurNAc. Plays a role in intrinsic resistance to fosfomycin, which
CC targets the de novo synthesis of UDP-MurNAc. Shows a very low activity
CC on GlcNAc-6P, and neither alpha-1-phosphorylated MurNAc, GlcNAc, or
CC glucose nor glucosamine-6P or glucose-6P can be used as a substrate.
CC {ECO:0000269|PubMed:28351914}.
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:0000269|PubMed:28351914};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28351914};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=310 uM for N-acetylmuramate 6-phosphate (at pH 7.6 and 22 degrees
CC Celsius) {ECO:0000269|PubMed:28351914};
CC Vmax=2.04 umol/min/mg enzyme (at pH 7.6 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:28351914};
CC Note=kcat is 0.88 sec(-1) (at pH 7.6 and 22 degrees Celsius).
CC {ECO:0000269|PubMed:28351914};
CC pH dependence:
CC Optimum pH is 6-9. At pH 4 and pH 10, its activity is only 40 and
CC 60%, respectively, of the maximum. {ECO:0000269|PubMed:28351914};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. However, at that
CC temperature, MupP is completely inactivated within 40 minutes. Loses
CC about 10% of its activity at 22 degrees Celsius and 70% at 37 degrees
CC Celsius within 40 minutes. {ECO:0000269|PubMed:28351914};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:28351914}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are highly susceptible to
CC fosfomycin, accumulate large amounts of MurNAc 6-phosphate, and show
CC lower levels of UDP-MurNAc and UDP-GlcNAc than wild-type cells.
CC {ECO:0000269|PubMed:28351914}.
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; AE015451; AAN67384.1; -; Genomic_DNA.
DR RefSeq; NP_743920.1; NC_002947.4.
DR RefSeq; WP_010952803.1; NC_002947.4.
DR AlphaFoldDB; Q88M11; -.
DR SMR; Q88M11; -.
DR STRING; 160488.PP_1764; -.
DR EnsemblBacteria; AAN67384; AAN67384; PP_1764.
DR KEGG; ppu:PP_1764; -.
DR PATRIC; fig|160488.4.peg.1859; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_1_6; -.
DR OMA; TPHAKPH; -.
DR PhylomeDB; Q88M11; -.
DR BioCyc; MetaCyc:G1G01-1865-MON; -.
DR BioCyc; PPUT160488:G1G01-1865-MON; -.
DR BRENDA; 3.1.3.105; 5092.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
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:0097172; P:N-acetylmuramic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IMP:UniProtKB.
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 PRINTS; PR00413; HADHALOGNASE.
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..223
FT /note="N-acetylmuramic acid 6-phosphate phosphatase"
FT /id="PRO_0000441264"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P95649"
SQ SEQUENCE 223 AA; 24373 MW; 64B0EA85BBA0DC57 CRC64;
MRLRAVLFDM DGTLLDTAPD FIAICQAMLA ERGLPAVDDN LIRGVISGGA RAMVATAFAM
DPEADGFEAL RLEFLERYQR DCAVHSKLFE GMAELLADIE KGNLLWGVVT NKPVRFAEPI
MQQLGLAERS ALLICPDHVK NSKPDPEPLI LACKTLNLDP ASVLFVGDDL RDIESGRDAG
TRTAAVRYGY IHPEDNPNNW GADVVVDHPL ELRKVIDSAL CGC
