PULA_STREE
ID PULA_STREE Reviewed; 1287 AA.
AC Q9F930;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pullulanase A {ECO:0000303|PubMed:11083842};
DE EC=3.2.1.41 {ECO:0000269|PubMed:11083842};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000305};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000305};
DE Flags: Precursor;
GN Name=spuA {ECO:0000303|PubMed:11083842, ECO:0000312|EMBL:AAG33958.1};
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000312|EMBL:AAG33958.1};
RN [1] {ECO:0000312|EMBL:AAG33958.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=3.B / Serotype 1 {ECO:0000303|PubMed:11083842,
RC ECO:0000312|EMBL:AAG33958.1};
RX PubMed=11083842; DOI=10.1128/iai.68.12.7141-7143.2000;
RA Bongaerts R.J., Heinz H.P., Hadding U., Zysk G.;
RT "Antigenicity, expression, and molecular characterization of surface-
RT located pullulanase of Streptococcus pneumoniae.";
RL Infect. Immun. 68:7141-7143(2000).
CC -!- FUNCTION: Virulence factor (By similarity). Involved in the degradation
CC of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-
CC branchpoints of glycogen (By similarity). Hydrolyzes pullulan
CC (PubMed:11083842). Does not hydrolyze dextran. Binds to mouse lung
CC alveolar type II cells that are rich in glycogen stores. Is an alpha-
CC glucan-specific carbohydrate-binding protein, which binds to amylose
CC (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked
CC glucose with alpha-(1,6) branch points), pullulan (linear polymer of
CC mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen
CC (similar to amylopectin with more frequent alpha-(1,6) branch points)
CC in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-
CC linked glucose) (By similarity). {ECO:0000250|UniProtKB:A0A0H2UNG0,
CC ECO:0000250|UniProtKB:A0A0H2ZL64, ECO:0000269|PubMed:11083842}.
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:0000269|PubMed:11083842};
CC -!- ACTIVITY REGULATION: Inhibited by 4-O-alpha-D-glucopyranosylmoranoline
CC (G1M). {ECO:0000250|UniProtKB:A0A0H2UNG0}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:11083842}.
CC Note=Localizes to cytoplasm in the lung alveolar type II cells of the
CC mouse and human hosts. {ECO:0000250|UniProtKB:A0A0H2UNG0}.
CC -!- DOMAIN: The N-terminal tandem family 41 carbohydrate-binding modules
CC (CBM) are involved in carbohydrate binding. The C-terminal glycosyl
CC hydrolase 13 (GH13) domain is involved in catalysis.
CC {ECO:0000250|UniProtKB:A0A0H2UNG0}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF217414; AAG33958.1; -; Genomic_DNA.
DR RefSeq; WP_001860626.1; NZ_FYSI01000010.1.
DR AlphaFoldDB; Q9F930; -.
DR SMR; Q9F930; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IC:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 2.60.40.1220; -; 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 Pfam; PF00128; Alpha-amylase; 2.
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; SSF49452; SSF49452; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02102; pullulan_Gpos; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell wall; Glycosidase; Hydrolase; Metal-binding;
KW Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1287
FT /note="Pullulanase A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451848"
FT PROPEP 1257..1287
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5025750514"
FT REGION 42..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1253..1257
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 42..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT ACT_SITE 814
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 270..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 674..675
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 750
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 816
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 835
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 838
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 846
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 849
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 856
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 889
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 893
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 903
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 976
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 996..998
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 999
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT SITE 902
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT MOD_RES 1256
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1287 AA; 143317 MW; ECFCA3E3D1ED73E4 CRC64;
MRKTPSHTEK KMVYSIRSLK NGTGSVLIGA SLVLLAMATP TISSDESTPT TNEPNNRNTT
TLAQPLTDTA AGSGKNESDI SSPGNANASL EKTEEKPATE PTTPAASPAD PAPQTGQDRS
SEPTTSTSPV TTETKAEEPI EDNYFRIHVK KLPEENKDAQ GLWTWDDVEK PSENWPNGAL
SFKDAKKDDY GYYLDVKLKG EQAKKISFLI NNTAGKNLTG DKSVEKLVPK MNEAWLDQDY
KVFSYEPQPA GTVRVNYYRT DGNYDKKSLW YWGDVKNPSS AQWPDGTDFT ATGKYGRYID
IPLNEAAREF GFLLLDESKQ GDDVKIRKEN YKFTDLKNHS QIFLKDDDES IYTNPYYVHD
IRMTGAQHVG TSSIESSFST LVGAKKEDIL KHSNITNHLG NKVTITDVAI DEAGKKVTYS
GDFSDTKHPY TVSYNSDQFT TKTSWRLKDE TYSYDGKLGA DLKEEGKQVD LTLWSPSADK
VSVVVYDKND PDKVVGTVAL EKGERGTWKQ TLDSTNKLGI TDFTGYYYQY QIERQGKTVL
ALDPYAKSLA AWNSDDAKID DAHKVAKAAF VDPAKLGPQD LTYGKIHNFK TREDAVIYEA
HVRDFTSDPA IAKDLTKPFG TFEAFIEKLD YLKDLGVTHI QLLPVLSYYF VNELKNHEHL
SDYASSNSNY NWGYDPQNYF SLTGMYSSDP KNPEKRIAEF KNLINEIHKR GMGAILDVVY
NHTAKVDIFE DLEPNYYHFM DADGTPRTSF GGGRLGTTHH MTKRLLVDSI KYLVDTYKVD
GFRFDMMGDH DAASIEEAYK AARALNPNLI MLGEGWRTYA GDENMPTKAA DQDWMKHTDT
VAVFSDDIRN NLKSGYPNEG QPAFITGGKR DVNTIFKNLI AQPTNFEADS PGDVIQYIAA
HDNLTLFDII AQSIKKDPSK AENYAEIHRR LRLGNLMVLT AQGTPFIHSG QEYGRTKQFR
NPAYRTPVAE DKVPNKSHLL RDKDGNPFDY PYFIHDSYDS SDAVNKFDWT KATDGKAYPE
NVKSRDYMKG LIALRQSTDA FRLKSLQDIK DRVHLITVPG QNGVEKEDVV IGYQITAPNG
DIYAVFVNAD EKAREFNLGT AFAHLRNAEV LADENQAGSV GIANPKGLEW TEKGLKLNAL
TATVLRVSQN GTSHESTAEE KPDSTPSKPE HQNEASHPAH QDPAPEARPD STKPDAKVAD
AENKPSQATA DSQAEQPAQE AQASSVKEAV RKESVENSSK ENISATPDRQ AELPNTGIKN
ENKLLFAGIS LLALLGLGFL LKNKKEN
