ID A0A0U2PJT1_9ALTE Unreviewed; 329 AA.
AC A0A0U2PJT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Secretion protein {ECO:0000313|EMBL:ALS99821.1};
GN ORFNames=AT746_17155 {ECO:0000313|EMBL:ALS99821.1};
OS Lacimicrobium alkaliphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Lacimicrobium.
OX NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS99821.1, ECO:0000313|Proteomes:UP000068447};
RN [1] {ECO:0000313|EMBL:ALS99821.1, ECO:0000313|Proteomes:UP000068447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YelD216 {ECO:0000313|EMBL:ALS99821.1,
RC ECO:0000313|Proteomes:UP000068447};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL Submitted (DEC-2015) 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; CP013650; ALS99821.1; -; Genomic_DNA.
DR RefSeq; WP_062482919.1; NZ_CP013650.1.
DR AlphaFoldDB; A0A0U2PJT1; -.
DR STRING; 1526571.AT746_17155; -.
DR KEGG; lal:AT746_17155; -.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000068447; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08990; GH43_AXH_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000068447};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006831772"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 159
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 329 AA; 37446 MW; DB09DD681C9A3AAC CRC64;
MLKLTIFTAA LVLFPVLVAA QNPLDFGSNI RTADPSAHVW EDGRLYLYTS HDIECQRDFH
MQDWHLFSTD DLQSWTAHGA VLSVDDLSWA DDYAWAPDAA YKNGKYYLIF PAGTGVKDRQ
NPQNSTKWMG IGVAVSDSPT GPFKDAIGGP LWREPYANDP ALFIDDDGSA YLYFHGKGFD
YYVAEMADDM LSVKGDFIKM DMGGYEPKME GPWVFKRDGL YYFTMPGNNR VLTYYTATQP
TGPWTYQGVF MEQEHASNNH HSVVEYKGQW LLFYHRWLKI DDAACDKRQR HVAAEYLHFN
QDGTIRPVQR TEQGLADVPP MADSARSQN
//
