PULA_STRP2
ID PULA_STRP2 Reviewed; 1256 AA.
AC A0A0H2ZL64;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Pullulanase A {ECO:0000305};
DE EC=3.2.1.41 {ECO:0000250|UniProtKB:A0A0H2UNG0};
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:0000305};
GN OrderedLocusNames=SPD_0250 {ECO:0000312|EMBL:ABJ53695.1};
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153 {ECO:0000312|EMBL:ABJ53695.1};
RN [1] {ECO:0000312|EMBL:ABJ53695.1, ECO:0000312|Proteomes:UP000001452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466 {ECO:0000312|Proteomes:UP000001452};
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21565699; DOI=10.1016/j.str.2011.03.001;
RA Lammerts van Bueren A., Ficko-Blean E., Pluvinage B., Hehemann J.H.,
RA Higgins M.A., Deng L., Ogunniyi A.D., Stroeher U.H., El Warry N.,
RA Burke R.D., Czjzek M., Paton J.C., Vocadlo D.J., Boraston A.B.;
RT "The conformation and function of a multimodular glycogen-degrading
RT pneumococcal virulence factor.";
RL Structure 19:640-651(2011).
CC -!- FUNCTION: Virulence factor (PubMed:17041037). Involved in the
CC degradation of glycogen of the mammalian host cells. Hydrolyzes the
CC alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not
CC hydrolyze dextran. Binds to mouse lung alveolar type II cells that are
CC rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-
CC binding protein, which binds to amylose (pure alpha-(1,4)-linked
CC glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6)
CC branch points), pullulan (linear polymer of mixed alpha-(1,4)- and
CC alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with
CC more frequent alpha-(1,6) branch points) in vitro. Does not bind to
CC dextran (a linear polymer of alpha-(1,6)-linked glucose) (By
CC similarity). {ECO:0000250|UniProtKB:A0A0H2UNG0,
CC ECO:0000269|PubMed:17041037}.
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:0000250|UniProtKB:A0A0H2UNG0};
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:0000250|UniProtKB:Q9F930}.
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 -!- DISRUPTION PHENOTYPE: Reduced numbers of pneumococci relative to wild-
CC type 48 hours post-infection in the lungs and blood of the mouse
CC infection model confirming a role for this protein in invasive disease.
CC {ECO:0000269|PubMed:17041037}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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; CP000410; ABJ53695.1; -; Genomic_DNA.
DR RefSeq; WP_001232763.1; NC_008533.2.
DR AlphaFoldDB; A0A0H2ZL64; -.
DR SMR; A0A0H2ZL64; -.
DR STRING; 373153.SPD_0250; -.
DR EnsemblBacteria; ABJ53695; ABJ53695; SPD_0250.
DR GeneID; 60232440; -.
DR KEGG; spd:SPD_0250; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_0_0_9; -.
DR OMA; KMNEVWI; -.
DR OrthoDB; 99080at2; -.
DR BioCyc; SPNE373153:G1G6V-274-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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..1256
FT /note="Pullulanase A"
FT /evidence="ECO:0000255"
FT /id="PRO_5002603613"
FT PROPEP 1226..1256
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5018356435"
FT REGION 42..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1222..1226
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 42..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 763
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT ACT_SITE 792
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 652..653
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 728
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 813
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 816
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 817
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 824
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 827
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 834
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 867
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 871
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 881
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 954
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 974..976
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT BINDING 977
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT SITE 880
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:A0A0H2UNG0"
FT MOD_RES 1225
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1256 AA; 140279 MW; 62CC8A2D4F3C49AA CRC64;
MRKTPSHTEK KMVYSIRSLK NGTGSVLIGA SLVLLAMATP TISSDESTPT TNEPNNRNTT
TLAQPLTDTA ADSGKNESDI SSPRNANASL EKTEEKPATE PTTSTSPVTT ETKAEEPIED
NYFRIHVKKL PEENKDAQGL WTWDDVEKPS ENWPNGALSF KDAKKDDYGY YLDVKLKGEQ
AKKISFLINN TAGKNLTGDK SVEKLVPKMN EAWLDQDYKV FSYEPQPAGT VRVNYYRTDG
NYDKKSLWYW GDVKNPSSAQ WPDGTDFTAT GKYGRYIDIP LNEAAREFGF LLLDESKQGD
DVKIRKENYK FTDLKNHSQI FLKDDDESIY TNPYYVHDIR MTGAQHVGTS SIESSFSTLV
GAKKEDILKH SNITNHLGNK VTITDVAIDE AGKKVTYSGD FSDTKHPYTV SYNSDQFTTK
TSWHLKDETY SYDGKLGADL KEEGKQVDLT LWSPSADKVS VVVYDKNDPD KVVGTVALEK
GERGTWKQTL DSTNKLGITD FTGYYYQYQI ERQGKTVLAL DPYAKSLAAW NSDDAKIDDA
HKVAKAAFVD PAKLGPQDLT YGKIHNFKTR EDAVIYEAHV RDFTSDPAIA KDLTKPFGTF
EAFIEKLDYL KDLGVTHIQL LPVLSYYFVN ELKNHERLSD YASSNSNYNW GYDPQNYFSL
TGMYSSDPKN PEKRIAEFKN LINEIHKRGM GAILDVVYNH TAKVDIFEDL EPNYYHFMDA
DGTPRTSFGG GRLGTTHHMT KRLLVDSIKY LVDTYKVDGF RFDMMGDHDA ASIEEAYKAA
RALNPNLIML GEGWRTYAGD ENMPTKAADQ DWMKHTDTVA VFSDDIRNNL KSGYPNEGQP
AFITGGKRDV NTIFKNLIAQ PTNFEADSPG DVIQYIAAHD NLTLFDIIAQ SIKKDPSKAE
NYAEIHRRLR LGNLMVLTAQ GTPFIHSGQE YGRTKQFRDP AYKTPVAEDK VPNKSHLLRD
KDGNPFDYPY FIHDSYDSSD AVNKFDWTKA TDGKAYPENV KSRDYMKGLI ALRQSTDAFR
LKSLQDIKDR VHLITVPGQN GVEKEDVVIG YQITAPNGDI YAVFVNADEK AREFNLGTAF
AHLRNAEVLA DENQAGSVGI ANPKGLEWTE KGLKLNALTA TVLRVSQNGT SHESTAEEKP
DSTPSKPEHQ DPAPEARPDS TKPDAKVADA ENKPSQATAD SQAEQPAQEA QASSVKEAVQ
NESVENSSKK NIPATPDRQA ELPNTGIKNE NKLLFAGISL LALLGLGFLL KNKKEN
