ID   MUPG_STAA3              Reviewed;         351 AA.
AC   A0A0H2XHV5;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=6-phospho-N-acetylmuramidase {ECO:0000303|PubMed:30524387};
DE            EC=3.2.1.- {ECO:0000269|PubMed:30524387};
DE   AltName: Full=MurNAc 6P-GlcNAc glycosyl hydrolase {ECO:0000305|PubMed:30524387};
DE   AltName: Full=MurNAc-6P glycosidase {ECO:0000303|PubMed:30524387};
GN   Name=mupG {ECO:0000303|PubMed:30524387};
GN   OrderedLocusNames=SAUSA300_0192 {ECO:0000312|EMBL:ABD22197.1},
GN   NRS_202 {ECO:0000312|EMBL:AVM10979.1};
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / NRS384;
RA   Date S.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=USA300;
RX   PubMed=30524387; DOI=10.3389/fmicb.2018.02725;
RA   Kluj R.M., Ebner P., Adamek M., Ziemert N., Mayer C., Borisova M.;
RT   "Recovery of the Peptidoglycan Turnover Product Released by the Autolysin
RT   Atl in Staphylococcus aureus Involves the Phosphotransferase System
RT   Transporter MurP and the Novel 6-phospho-N-acetylmuramidase MupG.";
RL   Front. Microbiol. 9:2725-2725(2018).
CC   -!- FUNCTION: Involved in the recycling pathway of the cell wall turnover
CC       product MurNAc-GlcNAc in S.aureus. Catalyzes the hydrolysis of MurNAc
CC       6-phosphate-GlcNAc, the disaccharide product of MurP-uptake and
CC       phosphorylation, yielding MurNAc 6-phosphate and GlcNAc.
CC       {ECO:0000269|PubMed:30524387}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-N-acetyl-beta-D-muramate-(1->4)-N-acetyl-D-
CC         glucosamine + H2O = N-acetyl-D-glucosamine + N-acetyl-D-muramate 6-
CC         phosphate; Xref=Rhea:RHEA:66780, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58722, ChEBI:CHEBI:167477, ChEBI:CHEBI:506227;
CC         Evidence={ECO:0000269|PubMed:30524387};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66781;
CC         Evidence={ECO:0000269|PubMed:30524387};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000305|PubMed:30524387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:30524387}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a cytoplasmic
CC       accumulation of MurNAc 6-phosphate-GlcNAc, predominantly during
CC       stationary phase. This accumulation can be abolished by expressing
CC       MupG. {ECO:0000269|PubMed:30524387}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 170 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000255; ABD22197.1; -; Genomic_DNA.
DR   EMBL; CP027476; AVM10979.1; -; Genomic_DNA.
DR   RefSeq; WP_000145555.1; NZ_CP027476.1.
DR   AlphaFoldDB; A0A0H2XHV5; -.
DR   SMR; A0A0H2XHV5; -.
DR   EnsemblBacteria; ABD22197; ABD22197; SAUSA300_0192.
DR   KEGG; saa:SAUSA300_0192; -.
DR   HOGENOM; CLU_065324_0_0_9; -.
DR   OMA; QDCGVDK; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR008589; MupG.
DR   InterPro; IPR043894; MupG_C.
DR   InterPro; IPR043797; MupG_N.
DR   PANTHER; PTHR38435; PTHR38435; 1.
DR   Pfam; PF05913; DUF871; 1.
DR   Pfam; PF19200; DUF871_N; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..351
FT                   /note="6-phospho-N-acetylmuramidase"
FT                   /id="PRO_0000452698"
SQ   SEQUENCE   351 AA;  40360 MW;  2CCBFBC51F400971 CRC64;
     MTGFSVYLGQ PLDEAYIKRM IKQGYQMIFT SVQIPEEDDE TKYHYFTKLL NLLKHEQVTY
     LIDANPSILT PSFYDHLRQY DAQFMIRIDH STSIEAIEAI MAQGLKCCLN ASIISRELLT
     SLHQQLNDFT LLSFCHNYYP RPDTGLSVDL VNKKNELIYQ FNPKAQIYGF IVGSDLRGPL
     HKGLPTIEAT RHSHPVVAAK LLQETGVSEV LVGDSLIEMR QAKQLIDFCK HRHFTLCIEE
     VFDTTVTYLF DMCHKVRPDN PENVIRSETS RQICPHSIQP QFTTQRRIGS VTVDNLNNGR
     YQGEMQIVRQ TLSAHDNVNV VAQIIKEDLP LLSCIEPNDT FDFQKTRECK K