ID U4THT6_9LACO Unreviewed; 349 AA.
AC U4THT6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERL63734.1};
GN ORFNames=L248_2231 {ECO:0000313|EMBL:ERL63734.1};
OS Schleiferilactobacillus shenzhenensis LY-73.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL63734.1, ECO:0000313|Proteomes:UP000030647};
RN [1] {ECO:0000313|Proteomes:UP000030647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX PubMed=24265500;
RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA Yang R., Liu F.;
RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL Genome Announc. 1:e00972-e00913(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KI271616; ERL63734.1; -; Genomic_DNA.
DR AlphaFoldDB; U4THT6; -.
DR STRING; 1231336.L248_2231; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_009397_2_2_9; -.
DR Proteomes; UP000030647; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_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};
KW Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 165
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 349 AA; 38497 MW; 3321617FEC9D13DE CRC64;
MNNKAGMQKL ILAVIATMVL LIGGCALNTK TSTKTVTFTN PLSTDGGVYS DPWLIRVGKE
YYYCGSDGKS QITIKKSNAP TDILEQNDHV VWQAPDRSSY SSETWAPELH YLSGRWYIYF
AADDGENANH RMYALAGGTN FNDPLDGKYS FQGKVADDTN RWAIDGTVLT IAKKLYFVWS
GWAGEQNVAQ NLYIAPMSDP VTISGTRVLI SAPTEPWERN GEPFVNEGPE VLTHEGQVTL
IYSASGSWTD NYCLGQLTLK GKNPLKPSNW VKRKSGPVFK KTNQVFGPGH ASFISSPDGT
PWIMYHAAKV KGSGWDRDIR LQPFSWNSDG TPSFGKPEAP GKKISYSLN
//