ID A0A0L0LBU7_9BACT Unreviewed; 426 AA.
AC A0A0L0LBU7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Spore peptidoglycan hydrolase (N-acetylglucosaminidase) {ECO:0000313|EMBL:KND47486.1};
GN ORFNames=AB199_03590 {ECO:0000313|EMBL:KND47486.1};
OS Parcubacteria bacterium C7867-004.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659198 {ECO:0000313|EMBL:KND47486.1, ECO:0000313|Proteomes:UP000036787};
RN [1] {ECO:0000313|EMBL:KND47486.1, ECO:0000313|Proteomes:UP000036787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-004 {ECO:0000313|EMBL:KND47486.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000256|RuleBase:RU004453}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KND47486.1}.
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DR EMBL; LFCN01000006; KND47486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LBU7; -.
DR STRING; 1659198.AB199_03590; -.
DR Proteomes; UP000036787; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR46066:SF2; CHITINASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46066; CHITINASE DOMAIN-CONTAINING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005543552"
FT DOMAIN 47..426
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 426 AA; 46627 MW; F81C51FA5CCD7692 CRC64;
MHVLFFKLAT LSLLAAVILT SAAPLSASAA SSSKKGETKS TKEASGKLEV SGWIPYWRTD
AGTRDASAHL SQLTEVNPFG YTVKADGTLN DAANIQSRAW QDLFKAAKAK KVRVIPTVMW
SDTDAIHKVL SDPKKRAAHI QSIVKAVNDN GFDGIDIDYE GKKAETRTYY SAFLKELAAE
FGKKKSNKWL MCTIEARMPL EARFSGTPPA NIEYANDFKE INTYCDRVRV MTYDQQTADL
QLNAAARAAN EAYAPVADVK WVEKVINYMA KDIDKKKMSI GIATYGYIYQ LMPYTDGSGF
NYIKTEAFNP AYATDIAAKY GITPTRNRAG ELSFTYVPKE QVSALPNQGF LAALAPRGTT
SGNLAAAGAL ALAKKDKKQA PVQLLWWSDA KAIGDKVALA KKLKVAGVSV FKFDGGSDPK
MWDYLK
//