ID   G7VZX1_PAETH            Unreviewed;      1141 AA.
AC   G7VZX1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=beta-amylase {ECO:0000256|ARBA:ARBA00012594};
DE            EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594};
GN   OrderedLocusNames=HPL003_06095 {ECO:0000313|EMBL:AET57982.1};
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=985665 {ECO:0000313|EMBL:AET57982.1, ECO:0000313|Proteomes:UP000005876};
RN   [1] {ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AET57982.1, ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|EMBL:AET57982.1,
RC   ECO:0000313|Proteomes:UP000005876};
RX   PubMed=22328761; DOI=10.1128/JB.06668-11;
RA   Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA   Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT   "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT   Bacterium Isolated from Soil Found in Forest Residue.";
RL   J. Bacteriol. 194:1266-1266(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive maltose units from the
CC         non-reducing ends of the chains.; EC=3.2.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000546};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600125-3};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR600125-3};
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; CP003107; AET57982.1; -; Genomic_DNA.
DR   RefSeq; WP_014278733.1; NC_016641.1.
DR   AlphaFoldDB; G7VZX1; -.
DR   STRING; 985665.HPL003_06095; -.
DR   KEGG; pta:HPL003_06095; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_279379_0_0_9; -.
DR   Proteomes; UP000005876; Chromosome.
DR   GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11339; AmyAc_bac_CMD_like_2; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR000125; Glyco_hydro_14A_bac.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF03423; CBM_25; 2.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00841; GLHYDLASE14A.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01066; CBM_25; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR600125-3};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR600125-3};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1141
FT                   /note="beta-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003504737"
FT   DOMAIN          459..537
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          569..647
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          696..1052
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          1064..1141
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   REGION          546..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-1"
FT   ACT_SITE        394
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-1"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         170
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         395..396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
SQ   SEQUENCE   1141 AA;  124999 MW;  0D6B8FD0AAC1E80C CRC64;
     MTLYRSLWNK GCLILLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA KINDWGAFKK
     QLQTLKSNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAD AVKEVGLKWV PIISTHKCGG
     NVGDDCNIPL PSWLSSKGSA DEMQFKDESG YANNEALSPL WSGAGKQYDE LYASFAENFA
     GYKSIIPKIY LSGGPSGELR YPSYYPAAGW SYPARGKFQA YTETAKNAFR AAMNEKYGSL
     DKINAAWGTK LSSLSQINPP SDGDGFYTNG GYNSTYGKDF LSWYQSVLEN HLGVIGAAAH
     KNFDSVFGVR IGAKISGLHW QMNNPAMPHS TEHAGGYYDY NRLIQKFKDA DLDLTFTALE
     MNDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG GSGFQKIEEK ITKFGYHGFT
     LLRINNLVNS DGSPTGELDG FKQYIISKAK PGDNGGGTGN KVTIYYKKGF NSPYIHYRPA
     GGNWTAVPGV KMQDAEISGY AKITVDIGSA SQLEAAFNDG NNNWDSNNTK NYLFSTGTST
     YTPGDTSKAG TITSGTPSGT NPGEGGGTTN KVTIYYKKGF NSPYIHYRPA GGNWTAVPGV
     KMQDAEISGY AKITVDIGSA SQLEAAFNDG NNNWDSNNTK NYFFTTGTST YTPGSNGAAG
     TVQTGSPSGG STPTDPESPS NPTPLSTDWS KQSIYFIMTD RFSNGDTSND NYGGFNSNNS
     DMRKWHGGDF QGIINQLDYI QNMGFTAIWI TPVTMQKSEF AYHGYHTYDF YAVDGHLGTM
     DKFKELIRKA HDKNIAVMLD VVVNHTGDFQ PANGFAKAPF DKADWYHHNG DITGADYSSN
     NQTKIENGDV AGLDDLNQDN PATANELKNW IKWLLNESGV DGLRVDTAKH VPKGFLKDFD
     QAANTFTIGE IYSGDPAYVG DYTRYLDAAL DFPMYYTIKD VFGRDQSMIK IKERYSDDRY
     YRDAQTNGVF IDNHDVKRFL NEASGKPGAS SDKWPQLKAA LGFTLTSRGI PIIYQGTEQG
     FSGGDDPANR ENVVFNANHE LYQYIAKLNR VRNSHPALQN GSQKEKWADD SFYSFQRSKN
     GDEAIVLINN SWSSQTRTIS NFDNLSNGTR LTNQLSNDSI QINNGSITVT LAPKEVKIFT
     R
//