LPQI_MYCTU
ID LPQI_MYCTU Reviewed; 388 AA.
AC L7N6B0; I6Y775;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Beta-hexosaminidase LpqI {ECO:0000305};
DE EC=3.2.1.52 {ECO:0000269|PubMed:31201321};
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=Rv0237 {ECO:0000312|EMBL:CCP42966.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 44-386, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBCELLULAR LOCATION.
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:0000269|PubMed:31201321}.
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:0000269|PubMed:31201321};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72 uM for 4MU-GlcNAc {ECO:0000269|PubMed:31201321};
CC Note=kcat is 0.02 sec(-1) with 4MU-GlcNAc as substrate.
CC {ECO:0000269|PubMed:31201321};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:31201321}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:31201321}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Periplasmic side {ECO:0000305|PubMed:31201321}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP42966.1; -; Genomic_DNA.
DR RefSeq; WP_003401295.1; NZ_NVQJ01000001.1.
DR RefSeq; YP_177702.1; NC_000962.3.
DR PDB; 6GFV; X-ray; 1.96 A; A/B=44-386.
DR PDBsum; 6GFV; -.
DR AlphaFoldDB; L7N6B0; -.
DR SMR; L7N6B0; -.
DR STRING; 83332.Rv0237; -.
DR PaxDb; L7N6B0; -.
DR PRIDE; L7N6B0; -.
DR GeneID; 886693; -.
DR KEGG; mtu:Rv0237; -.
DR PATRIC; fig|83332.111.peg.270; -.
DR TubercuList; Rv0237; -.
DR eggNOG; COG1472; Bacteria.
DR OMA; WQMAAEM; -.
DR PhylomeDB; L7N6B0; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001584; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; 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_5010230425"
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"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6GFV"
FT TURN 131..137
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6GFV"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:6GFV"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6GFV"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:6GFV"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:6GFV"
FT HELIX 366..380
FT /evidence="ECO:0007829|PDB:6GFV"
SQ SEQUENCE 388 AA; 39519 MW; 613649EF62E97503 CRC64;
MAFPRTLAIL AAAAALVVAC SHGGTPTGSS TTSGASPATP VAVPVPRSCA EPAGIPALLS
PRDKLAQLLV VGVRDAADAQ AVVTNYHVGG ILIGSDTDLT IFDGALAEIV AGGGPLPLAV
SVDEEGGRVS 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
