ID A0A249DGM7_LACRH Unreviewed; 1794 AA.
AC A0A249DGM7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:ASX18296.1};
GN ORFNames=BGK71_13100 {ECO:0000313|EMBL:ASX18296.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:ASX18296.1, ECO:0000313|Proteomes:UP000215843};
RN [1] {ECO:0000313|EMBL:ASX18296.1, ECO:0000313|Proteomes:UP000215843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LR5 {ECO:0000313|EMBL:ASX18296.1,
RC ECO:0000313|Proteomes:UP000215843};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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DR EMBL; CP017063; ASX18296.1; -; Genomic_DNA.
DR RefSeq; WP_049170834.1; NZ_VRTQ01000006.1.
DR GeneID; 69830459; -.
DR Proteomes; UP000215843; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd08759; Type_III_cohesin_like; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07554; FIVAR; 4.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1766..1784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 896..979
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 978..1129
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1135..1206
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT REGION 1696..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1668..1695
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1702..1734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1794 AA; 195073 MW; 17C15DF11B65002C CRC64;
MHNGMKTVKD RPRVPRSLLY SSAVLSLTAT VVYVSSTVPV TAAKGSEPAK SSAVKKASTS
MLNIVNVTKQ THYFEVTYSN NLKARVFILA NNQFRFYADP SGKFAAPAQS EKGLNAKIFT
KEIDASAAKA FAAATLDHNG DGWTIKTDAI AIGFNQANAT LQVSKGSKVV MAESQPLEIT
NDHATQVLKR GTDQFFGGGT QNGNFTLTGK NVKIENTGNW VDGGVASPNP FYWSTAGYGV
VRNTFKPGNY DFGASDDGQV TTTHQENRFD AVYFFDAKPY DLLKDYYDLT GAPAMMPRYG
LYEAHLNAYN RDTWVPVPEG TSGAIKFEDG KYYKEYQPGK IPAGQSGIKE SLNGELNNYQ
FSARAVIDRY QKNDMPLGWF LPNDGYGAGY GQTDTLAGNL QNLKSFADYA EQHGVATGLW
TQQNLSPVDP ANPKPDDRDF AKEVAIGVKA LKTDVAWVGS GYSFGLDGLA KADAMMTQVK
GDSLRPFAIT LDGWAGTQRY AGVWTGDQTG GQWEYIRFHI PTYIGTGLSG QPYVGSDMDG
IFGGGNPIVN TRDFQWKAFT PIQLNMDGWG ANPKTPFSFD QQTTAINRAY NKQKTMLMPY
NYTASAQSVF DGKPMVRGLF LDYPNIPEAY TDLVKYEYLW GDNFLVAPIY QNTAADEKGN
DVRNGIYLPD KQQVWVDYYT GKEYRGGQVL NNFEAPIWKL PVFVKKGAVI PTTPAHNTPK
AFDQTKRQFQ IFPASGKNDF TVYEDDGISK KYLKGAHAQA KVTSELQKDQ LTVNVDPLTG
DYSGLNPDRA TEFAIRTSGK PAKVTASVGG QTVKLTAVDN LKDFTAGENV YFVNKQYHTN
DFLDQLADKS IDQNFLQVKL GKTNVKSNAI KLTVDGIDAA DDPTTEALPE SDDVAVPTEI
KQNDQTTTGT TVGIDWKPVK DATSYDVKAD GVVYRNLTKP EFLLTPVKSQ TKHTFQVRAA
TAKAVSKWSN EQTFSSKDNP LRLAVKMSNP QVTSPITGVA TWQGKDTAAH LFDQDLTTMA
HSNWFTTPPK QSATPMTITT ELDGVYDLDH VTYVPREDGG NGTLSALKVE TSLDGIHWHQ
AGEGKGWTWD GKDKTITFDK NEKAQYVRFV IPKGTSRGDF VSGRELLLFK RDGSSKAVLG
DITNDGRVNE DDQTSLMNYA GLTANIDSDF NGYVQNGDLN RNGVIDAFDI NYVMTKLGKT
PVTKPDEQAP AGTLALEAEK QTHLPGETIT LNLLGKDLAN VNSLFARVPL TNPNVELVKV
EPTQATAQMV NFSKTRTHGD NSRDLYLIFA NEGQQKRLSG DQKLATITLR AKTRMTKAAL
SFALSDPMLT NQWGPENLPQ VPAPITILPA DTSALDQSRA QLNALIDGVN ALDPKLFTAA
SWQAVTAQRD RVSQVLDADN VTVDALNQAY ADLKHALGKL EADRGVTQDQ LKKLIEAAEA
LKADQYTAES FAKLTDAVAT AKPVSADANA TQAQIQAAIQ AISNAWFALE VKQQPQATTL
EQWVKVAANL NAADYTPNSF TQLTTVLDEA KKALTDPTTS AATQQKLADQ LQGAIDALVP
RADKQSLAAL VKATEKLKAS DYTASSYAKL QTALKPARLV LNDPNAAQAE VGKQADALMA
AMLQLEKQPD KTELVSLITK AAEFKAEAYT DTSFADLKTA LAQARAVNKD SEASVAKVEA
AVANLKAAID HLVKAAPTPE PDKDPHNPPV PTPGPGKDPS TPSNPEPGIP PKDKTPQPHA
GFNGESADTH KSTKNRDQMP NAGDRAQPVL AVIGAALIGL LGYVKLRQHH KNND
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