ID   H0E753_9ACTN            Unreviewed;       477 AA.
AC   H0E753;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Endo-14-beta-glucanase {ECO:0000313|EMBL:EHN10498.1};
GN   ORFNames=PAI11_26550 {ECO:0000313|EMBL:EHN10498.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10498.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN10498.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN10498.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|RuleBase:RU361153}.
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:EHN10498.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGUD01000217; EHN10498.1; -; Genomic_DNA.
DR   RefSeq; WP_007575944.1; NZ_AGUD01000217.1.
DR   AlphaFoldDB; H0E753; -.
DR   OrthoDB; 182870at2; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..477
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003532150"
FT   DOMAIN          75..337
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          458..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  51289 MW;  A00996AB35170612 CRC64;
     MFTVRRSIRS LLLAVVAVLL AAAPATAAPT PKVDGNRLVD TTTGSAFVPR GVNWPSFEYA
     CHYGYAYANE AGPATVGPTD EQARLIASWH ANVVRVPLNQ DCWLGDDGHP AGGLSADGYR
     NAVADWVSRL HAAGLAVILD LHWSGPDGVA ADGQRMLADD RSPAFWTSVA TRFRDDPSVL
     FDAFNEPFSQ SFDDGTTVPL DWACWSNGGC PAPRQNDGAG AFDGQTFTTT GMRALVAAIR
     GAGAQQPILL GGLDYANDLR GWLAARPDDG QLVASFHNYN GQRCQDQACW DAEIAPVAAQ
     VPVVTGEFGE TDCKDTHDRR YMDWADAHGV GYLAWQWVVL APNERATPAC ASLTLINDVQ
     GTPAAPNGTA LHDHLAQLAG AKPGDRRAPR PTRIQLRRTG RGLAVRLRLD EAATVRATLT
     RRGSDRRTVV SRRLGRGTRL LTLLRRRPAP GRYRVSLRAT DAAGNRSPAK SASLTVR
//