ID I0S9Y3_STRAP Unreviewed; 1273 AA.
AC I0S9Y3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=pullulanase {ECO:0000256|ARBA:ARBA00024062};
DE EC=3.2.1.41 {ECO:0000256|ARBA:ARBA00024062};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000256|ARBA:ARBA00029618};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000256|ARBA:ARBA00031076};
GN ORFNames=HMPREF1043_2393 {ECO:0000313|EMBL:EID20186.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID20186.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID20186.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID20186.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan,
CC amylopectin and glycogen, and in the alpha- and beta-limit dextrins
CC of amylopectin and glycogen.; EC=3.2.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00023965};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID20186.1}.
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DR EMBL; AICP01000056; EID20186.1; -; Genomic_DNA.
DR RefSeq; WP_003037695.1; NZ_AICP01000056.1.
DR AlphaFoldDB; I0S9Y3; -.
DR PATRIC; fig|1095729.3.peg.1848; -.
DR Proteomes; UP000003245; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011838; Pullulan_Gpos.
DR InterPro; IPR040806; SpuA_C.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR02102; pullulan_Gpos; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF18033; SpuA_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1250..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1243..1273
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 141352 MW; 976B4A4D1BF7AB85 CRC64;
MKKVYRLQSR TAEKRQHFGI RRLKVGVASI AISASVFLAG NVLAQAEEAN SVENISIETV
QPTSPTSERS DKVEVTNHQA VVSEKSENQE QASSSLLSTS SVANSLRTAL NEESSSEKLD
LTQAHSVREN TPALTTDSST EAQATKKETA QAAEEKTATK PVEKAASAAT PAKEDKIEEG
SIRLHFKTLP SENLASLGLW TWDDVETPSS QKGSWPTGAT SFSTAKKDDY GYYLDIKMAQ
KRSKISLLIN NTAGTNLTGD KTIELLSPNM NEVWFDKDYN LHTYEPLKEG MVRINYYRTD
GNYDKKSLWL WGDVENPSKN WPDGVDFEKT GKYGRYVDVP LKDAAKAIGF LLLDESKSGD
DVKIQPQDYN LTNLKKNSQI FLRDADPNIY TNPYFVNDIR MTGAQHIGLT EIEATFSTLE
NAKKEDILKN LKITDKDSKE VVVKDIVLDP KTKKAKIIGD FGQAQAPYTV KYGNDQFKTS
MNWQLKDSLY KYDGELGARV SQKGTKVDVT FWSPSADQVD LVVYDKNDQN KVVGKVAMTK
GEAGTWRTTL TSQTNLEIKD YRGYFYHYEI TRGDKKVLAL DPYAKSLAAW NSEDAEKGES
YKIAKAAFVD PSELGPKNLT YANIPGFKSR EDAVIYETHV RDFTSDATIS KDLKSQFGTF
SAFVEKLDYL KELGVTHIQL LPVLSYYFVN ELKNAERLDK YASSNSNYNW GYDPQNYFSL
TGMYSTNPTD PAKRIEEFKN LVHEIHKRGM GVIMDVVYNH TAKTSIFEDL EPNYYHFMDA
DGTPRTSFGG GRLGTTHYMS RRVLVDSIKY LTSEYKVDGF RFDMMGDHDA ESIQKAYEEA
KKLNPNLVML GEGWKTYAGD ENKPVQPADQ SWMKSTDTVG VFSDDIRNTL KSGYPNEGAP
AFITGGKRNV EDVFKNIKAQ PTNFEADDPG DVIQYIAAHD NLTLFDVIAQ SIKKDPAIAA
NNQEIHRRLR LGNLMILTSQ GTSFLHSGQE YGRTKQFRDP AYKYTVSEDK VPNKSHLLTN
ADGTPFEYPY FIHDSYDSSD AVNHFDWTKA TNGDKFPENT KSRDYVKGLI ALRKSTDAFT
RKTKAEVDQN VTLITQPGKD GVEKEDTVLG YQVVASNGDI YAVFVNADSK KRKFNFGEAY
RHLANAQVVA DGNTAGVTAI SNPAGVALGA DGVTLAPLTA TILRIQKNSK PNQEKPKEEQ
NQTKPSTPKG ESGQTTTSST QSNTSASQTQ QQQAGAGKAD KTLPSTGTTI SIAGVLAGIG
LLLSSVVVLK KKK
//
