ID A0A1D8ATQ9_9BACT Unreviewed; 350 AA.
AC A0A1D8ATQ9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase {ECO:0000313|EMBL:AOS44250.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:AOS44250.1};
GN ORFNames=Verru16b_01311 {ECO:0000313|EMBL:AOS44250.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS44250.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS44250.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS44250.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP016094; AOS44250.1; -; Genomic_DNA.
DR RefSeq; WP_069961519.1; NZ_CP016094.1.
DR AlphaFoldDB; A0A1D8ATQ9; -.
DR STRING; 1838286.Verru16b_01311; -.
DR KEGG; obg:Verru16b_01311; -.
DR PATRIC; fig|1838286.3.peg.1320; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000095228; Chromosome.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18817; GH43f_LbAraf43-like; 1.
DR InterPro; IPR016828; Alpha-L-arabinofuranosidase.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:AOS44250.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:AOS44250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..350
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009105158"
FT REGION 327..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 160
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 350 AA; 39150 MW; 04CB93AE753EB7BB CRC64;
MPHPRLPQGF MLASFALGCL LCLPLCAHAT PAVDLPNPLI FQRADPHVLK HSDGFYYYMG
TAPEYDRLVL RRAPTLAGLP TAEEKVIWRK HPTGIMGAHI WAPEIYHLDG RWFIYFAAGE
AEKIWNIRIY VLENTAANPL EGEWIERGQL KTGWESFTLD ASTFEHRGRR YLLWAQQQPG
IPGNTNLYIA PMASPTTLAG PAVLLSKPEF DWEKVRYAVN EGPVVLKKNG RLFLTYSAAG
TGPEYCLGML TADENADLLD PQSWVKSPAP VFVTSETNRI YGPGHHGFTV AEDGVTDLIV
YHARSYEEIK GDPLKDPNRH TRVQAVRWRA DGTPDFGVPR PDDPIPTPGR
//
