ID Q839P8_ENTFA Unreviewed; 835 AA.
AC Q839P8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Glycosyl hydrolase, family 20 {ECO:0000313|EMBL:AAO79989.1};
GN OrderedLocusNames=EF_0114 {ECO:0000313|EMBL:AAO79989.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO79989.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO79989.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2] {ECO:0007829|PDB:7PUJ, ECO:0007829|PDB:7PUK}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 487-835 IN COMPLEX WITH CA(2+);
RP MG(2+) AND ZN(2+).
RX PubMed=35241669; DOI=10.1038/s41467-022-28722-w;
RA Garcia-Alija M., Du J.J., Ordonez I., Diz-Vallenilla A.,
RA Moraleda-Montoya A., Sultana N., Huynh C.G., Li C., Donahue T.C.,
RA Wang L.X., Trastoy B., Sundberg E.J., Guerin M.E.;
RT "Mechanism of cooperative N-glycan processing by the multi-modular
RT endoglycosidase EndoE.";
RL Nat. Commun. 13:1137-1137(2022).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; AE016830; AAO79989.1; -; Genomic_DNA.
DR RefSeq; NP_813917.1; NC_004668.1.
DR RefSeq; WP_002387476.1; NZ_KE136524.1.
DR PDB; 7PUJ; X-ray; 1.75 A; A=55-486.
DR PDB; 7PUK; X-ray; 2.69 A; A/C=55-486.
DR PDB; 7PUL; X-ray; 1.40 A; A=487-835.
DR AlphaFoldDB; Q839P8; -.
DR SMR; Q839P8; -.
DR STRING; 226185.EF_0114; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR EnsemblBacteria; AAO79989; AAO79989; EF_0114.
DR KEGG; efa:EF0114; -.
DR PATRIC; fig|226185.45.peg.146; -.
DR eggNOG; COG3469; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_372901_0_0_9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd06542; GH18_EndoS-like; 1.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR PROSITE; PS01095; GH18_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7PUJ, ECO:0007829|PDB:7PUK};
KW Calcium {ECO:0007829|PDB:7PUL};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAO79989.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0007829|PDB:7PUJ, ECO:0007829|PDB:7PUL};
KW Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}; Zinc {ECO:0007829|PDB:7PUJ}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 496..764
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7PUJ"
FT BINDING 661
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 710
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:7PUL"
FT BINDING 774
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:7PUL"
SQ SEQUENCE 835 AA; 94070 MW; 7035FD1245898442 CRC64;
MNGVQKGMVF KVGNNLSTRK GENRETIVSW LGLSLLVGLA FILFSLFHQP MISQANEPTQ
EKHFMVYYRA WRDKTMQGVN TTLPDENWLT MHDIPYGIDI VNVFSYVPKG QEALAQPFYD
TLKNEYAPAL HARGVRLVRG IDYSELLKVP YAGTTPTEAE FDAYAKELLT KFVDDLGIDG
LDIDMETRPS EKDIVLSNGV IRALSKYIGP KSGTDRPFLY DTNAEYLPPL QDVSDCFDFL
AYQQYGSDDQ RTQRALNNLS PVLNGERFVP GLTFPEEQDR NRWYDTKEPY MESNMYKVAR
YSYENNLGGM FLYALDRDGR TYNEDDLNQI KPSNLLWTKT AIAESKGVSL AEMKAAAQHY
LKRISYANTD LEAQNKAAEA VTQATTLYDV NKAILGGDYG QGISNTYDAE LEKGLLAIDL
TTLYRALDQA VTAIEKAESY TPETIQALQT TKETVATELA GKTYTAAQVT TWQTEVQTAL
DNLKEKQTQP LKSVFSIDAG RKYFSVEQLE ELVAKASQNG YTDVQLILGN DGLRFILDDM
SVNVNGKKYN HNRVSKAIQR GNNAYYNDPN GNALTQKEMD RLLAFAKARN INIIPVINSP
GHMDALLVAM EKLAIKNPAF DGSKRTVDLG NQKAVNFTKA IISKYVAYFS AHSEIFNFGG
DEYANDVDTG GWAKLQSSGR YKDFVAYAND LAKIIKDAGM QPMSFNDGIY YNSDDSFGTF
DPEIIISYWT AGWSGYDVAK PEYFVQKGHK IFNTNDAWYW VAGNVDSGIY QYDDALANMS
KKAFTDVPAG SPNLPIIGSI QCVWYDDPRR DYDFERIYTL MDTFSENYRE YMVVK
//
