LPQI_MYCBP
ID LPQI_MYCBP Reviewed; 388 AA.
AC A0A0H3M1P5;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Beta-hexosaminidase LpqI {ECO:0000305};
DE EC=3.2.1.52 {ECO:0000250|UniProtKB:L7N6B0};
DE AltName: Full=Beta-N-acetylglucosaminidase {ECO:0000303|PubMed:31201321};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000305};
DE Flags: Precursor;
GN Name=lpqI {ECO:0000303|PubMed:31201321};
GN OrderedLocusNames=BCG_0275 {ECO:0000312|EMBL:CAL70259.1};
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=31201321; DOI=10.1038/s41467-019-10586-2;
RA Moynihan P.J., Cadby I.T., Veerapen N., Jankute M., Crosatti M.,
RA Mukamolova G.V., Lovering A.L., Besra G.S.;
RT "The hydrolase LpqI primes mycobacterial peptidoglycan recycling.";
RL Nat. Commun. 10:2647-2647(2019).
CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from
CC peptidoglycan fragments. Acts as a regulator for GlcNAc-MurNAc levels
CC by cleaving disaccharides and allowing the breakdown of MurNAc.
CC {ECO:0000250|UniProtKB:L7N6B0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000250|UniProtKB:L7N6B0};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:31201321}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:L7N6B0}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:L7N6B0}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is devoid of beta-N-
CC acetylglucosaminidase activity and shows increased antibiotic and
CC lysozyme resistance. Mutant is unable to grow on soluble peptidoglycan
CC as a sole carbon source. {ECO:0000269|PubMed:31201321}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AM408590; CAL70259.1; -; Genomic_DNA.
DR RefSeq; WP_010950367.1; NC_008769.1.
DR AlphaFoldDB; A0A0H3M1P5; -.
DR SMR; A0A0H3M1P5; -.
DR KEGG; mbb:BCG_0275; -.
DR HOGENOM; CLU_008392_0_4_11; -.
DR OMA; WQMAAEM; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.300; -; 1.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosidase; Hydrolase; Lipoprotein;
KW Membrane; Palmitate; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..388
FT /note="Beta-hexosaminidase LpqI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002615385"
FT ACT_SITE 236
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT SITE 234
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P40406"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 388 AA; 39533 MW; 795649EA5889750A CRC64;
MAFPRTLAIL AAAAALVVAC SHGGTPTGSS TTSGASPATP VAVPVPRSCA EPAGIPALLS
PRDKLAQLLV VGVRDAADAQ AVVTNYHVGG ILIGSDTDLT IFDGALAEIV AGGGPLPLAV
SVDEEGGRLS RLRSLIGGTG PSARELAQTR TVQQVRDLAR DRGRQMRKLG ITIDFAPVVD
VTDAPDDTVI GDRSFGSDPA TVTAYAGAYA QGLRDAGVLP VLKHFPGHGR GSGDSHNGGV
TTPPLDDLVG DDLVPYRTLV TQAPVGVMVG HLQVPGLTGS EPASLSKAAV NLLRTGTGYG
APPFDGPVFS DDLSGMAAIS DRFGVSEAVL RTLQAGADIA LWVTTKEVPA VLDRLEQALR
AGELPMSAVD RSVVRVATMK GPNPGCGR
