ID   E3E7E7_PAEPS            Unreviewed;      1196 AA.
AC   E3E7E7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=beta-amylase {ECO:0000256|ARBA:ARBA00012594};
DE            EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594};
GN   Name=amyB7 {ECO:0000313|EMBL:ADO59158.1};
GN   ORFNames=PPSC2_24470 {ECO:0000313|EMBL:ADO59158.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO59158.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO59158.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO59158.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
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};
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DR   EMBL; CP002213; ADO59158.1; -; Genomic_DNA.
DR   RefSeq; WP_013373692.1; NC_014622.2.
DR   AlphaFoldDB; E3E7E7; -.
DR   STRING; 1406.LK13_11960; -.
DR   CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   KEGG; ppm:PPSC2_24470; -.
DR   PATRIC; fig|886882.15.peg.5182; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_279379_0_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000006868; 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   Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1196
FT                   /note="beta-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003168893"
FT   DOMAIN          458..536
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          568..646
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          751..1107
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          1119..1196
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   REGION          544..566
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   1196 AA;  130845 MW;  ECF2BA51376F9675 CRC64;
     MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA KINDWGSFKK
     QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN AVKEAGLKWV PIISTHKCGG
     NVGDDCNIPL PSWLSSKGSA DEMQFKDESG YANSEALSPL WSGTGKQYDE LYASFAENFA
     GYKSIIPKIY LSGGPSGELR YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL
     DKLNAAWGTK LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH
     KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA DLDLTFTCLE
     MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG GSGFQKIEEK ITKFGYHGFT
     LLRINNLVNN DGSPTGELSG FKQYIISKAK PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG
     GSWTAAPGVK MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY
     TPGNSGNAGT ITSGAPSGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK
     MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY TPGSNGAAGT
     IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ AEKLSGVSLN VSTSTYAPNS NGVEVTAQTE
     APSGAFTPMD LGTLSNPTSL NTDWSKQSIY FIMTDRFSNG DPSNDNYGGF NSNNNDQRKW
     HGGDFQGIID KLDYIKNMGF TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKFQE
     LVRKAHDKNI AVMLDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITGG DYDSNNQWKI
     ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF LKDFDQAANT
     FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD QSMRKIKDRY SDDRYYRDAQ
     TNGVFIDNHD VKRFLNDASG KPGANYDKWP QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD
     DPANRENMNF NANHDLYQYI AKLNNVRNNH PALQNGSQKE KWVDDSFYSF QRSKNGDEAI
     VFINNSWNSQ TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKIFTK
//