ID Q99XX8_STRP1 Unreviewed; 1165 AA.
AC Q99XX8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 153.
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 Name=pulA {ECO:0000313|EMBL:AAK34661.1};
GN OrderedLocusNames=SPy_1972 {ECO:0000313|EMBL:AAK34661.1};
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447 {ECO:0000313|EMBL:AAK34661.1, ECO:0000313|Proteomes:UP000000750};
RN [1] {ECO:0000313|EMBL:AAK34661.1, ECO:0000313|Proteomes:UP000000750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1
RC {ECO:0000313|Proteomes:UP000000750};
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K.,
RA Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., Qian Y.,
RA Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
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}.
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DR EMBL; AE004092; AAK34661.1; -; Genomic_DNA.
DR RefSeq; NP_269940.1; NC_002737.2.
DR AlphaFoldDB; Q99XX8; -.
DR SMR; Q99XX8; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 1314-HKU360_01796; -.
DR KEGG; spy:SPy_1972; -.
DR PATRIC; fig|160490.10.peg.1715; -.
DR HOGENOM; CLU_004744_0_0_9; -.
DR OMA; KMNEVWI; -.
DR EvolutionaryTrace; Q99XX8; -.
DR Proteomes; UP000000750; Chromosome.
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 NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR02102; pullulan_Gpos; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000000750};
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 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1133..1165
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 57..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 128866 MW; 7A293706D24F2010 CRC64;
MKKKVNQGSK RYQYLLKKWG IGFVIAATGT VVLGCTPSIL THQVAAKTIV GLARDEAQQG
DGNAKSGDGL QSSSKEAKPV LDSSSANPAS IAEHHLRMHF KTLPAGESLG SLGLWVWGDV
DQPSKDWPNG AITMTKAKKD DYGYYLDVPL AAKHRQQVSY LINNKAGENL SKDQHISLLT
PKMNEVWIDE NYHAHAYRPL KKGYLRINYH NQSGHYDNLA VWTFKDVKTP TTDWPNGLDL
SHKGHYGAYV DVPLKEGANE IGFLILDKSK TGDAIKVQPK DYLFKELDNH TQVFVKDTDP
KVYNNPYYID QVSLKGAEQT TPNEIKAIFT TLDGLDEDAV KQNIKITDKA GKTVAIDELT
LDRDKSVMTL KGDFKAQGAV YTVTFGEVSQ VARQSWQLKD KLYAYDGELG ATLAKDGSVD
LALWSPSADT VKVVVYDKQD QTRVVGQADL TKSDKGVWRA HLTSDSVKGI SDYTGYYYLY
EITRGQEKVM VLDPYAKSLA AWNDATATDD IKTAKAAFID PSKLGPTGLD FAKINNFKKR
EDAIIYEAHV RDFTSDKALE GKLTHPFGTF SAFVEQLDYL KDLGVTHVQL LPVLSYFYAN
ELDKSRSTAY TSSDNNYNWG YDPQHYFALS GMYSANPNDP ALRIAELKNL VNEIHKRGMG
VIFDVVYNHT ARTYLFEDLE PNYYHFMNAD GTARESFGGG RLGTTHAMSR RILVDSITYL
TREFKVDGFR FDMMGDHDAA AIEQAFKAAK AINPNTIMIG EGWRTYQGDE GKKEIAADQD
WMKATNTVGV FSDDIRNTLK SGFPNEGTAA FITGGAKNLE GLFKTIKAQP GNFEADAPGD
VVQYIAAHDN LTLHDVIAKS INKDPKVAEE EIHKRIRLGN TMILTAQGTA FIHSGQEYGR
TKQLLNPDYK TKASDDKVPN KATLIDAVAQ YPYFIHDSYD SSDAVNHFDW AKATDSIAHP
ISNQTKAYTQ GLIALRRSTD AFTKATKAEV DRDVTLITQA GQDGIQQEDL IMGYQTVASN
GDRYAVFVNA DNKTRKVVLP QAYRYLLGAQ VLVDAEQAGV TAIAKPKGVQ FTKEGLTIEG
LTALVLKVSS KTANPSQQKS QTDNHQTKTP DGSKDLDKSL MTRPKRAKTN QKLPKTGEAS
SKGLLAAGIA LLLLAISLLM KRQKD
//
