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Database: UniProt
Entry: R6SKI1_9LACO
LinkDB: R6SKI1_9LACO
Original site: R6SKI1_9LACO 
ID   R6SKI1_9LACO            Unreviewed;      1306 AA.
AC   R6SKI1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=BN628_01544 {ECO:0000313|EMBL:CDC58039.1};
OS   Ligilactobacillus ruminis CAG:367.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1263085 {ECO:0000313|EMBL:CDC58039.1, ECO:0000313|Proteomes:UP000018129};
RN   [1] {ECO:0000313|EMBL:CDC58039.1, ECO:0000313|Proteomes:UP000018129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:367 {ECO:0000313|Proteomes:UP000018129};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CDC58039.1}.
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DR   EMBL; CBFO010000087; CDC58039.1; -; Genomic_DNA.
DR   Proteomes; UP000018129; 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; 1.
DR   CDD; cd02860; E_set_Pullulanase; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005323; CBM41_pullulanase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011840; PulA_typeI.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; TIGR02104; pulA_typeI; 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; PF19258; KxYKxGKxW_sig; 1.
DR   Pfam; PF03714; PUD; 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; 1.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1281..1299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1271..1306
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          58..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1306 AA;  140721 MW;  ABF01C25E7388415 CRC64;
     MHNQDVVQEN WRMWKHGKQW LYASSAVLAM GIYMGLSTTT VQADTLSNTQ TTTTAVQSVA
     KPATATTTTT GTTNAEQSGT VAETDQVPSI DPAADQPTKT DVAISQTPAA TSTLTGEKDL
     QSSLETKTNQ STSSTKSVAV PEVAKTNPVV TSEKAKTATP KNSQVETPAP VTQPVSAPAQ
     VDTKTETTAP VPVKDTTKVI IHYQGDSSKW APYVWGLKPN GNGQQYDWTG TDDFGAYAEI
     DMDQNYQQLG VLIKGVDSWD KDGNGADRTV TVDANGKGEV WYRAGSDDAQ DVTPTYHDTT
     INVHYHDKNQ SAVNHYRVWT DKAGEAGAQT VDLNQTDANG NLLGTVQLTA ADFTTVYVQP
     VGADELTRAF TPVASDAATD IYVVAGDQQP YYTASFALQQ EMVTSAAMQT PTEVTVTIGK
     ALTAAEARQQ LSVAGHTVKD VTAIAPDATG RSKQFKLTTT TDLDIMTTNS VSFNGNAKVM
     DIGDYVRSQA FDNEYYYDGD DLGVTYSKQR TQIKLWAPTA NQIELRLYQQ HTADAAVTKT
     IAMQRGAKGV WTAVLPGDYQ GWAYDYQLHF GDGSVTTTED PYSKAVTVNG NRSVIADVDA
     VKPADFDRLP SFSDPTDAVI YETSVRDFTK DPNSGVTAKG KFTGMVESGT HTASGQATGL
     DYLKDLGVTH VQLMPMYDFA SIDETSADPS YNWGYDPKNY NVPEGTYSSD ASDPTARVLE
     MKEMVNGYHK AGIRVVMDVV YNHVYSMDEQ AFQKVVPGYY FQYDQGGHPT SGSGVGNDVA
     SERRMVRKYI LDSVKYWATE YNIDGFRFDL MGILDVDTMN AIRAELNAID PGILVYGEGW
     DMRATNYDIG AGQYNADKLD QHIGFFSGDI RDAIRGAEFG GISKGLVEGN AQEDDYDQHA
     QAFIAGFLGG QDYANAVPAH PYQSPSQTLN YVACHDNRTL YDMLTALMPN ESQANLIKRD
     KLATSMAFLA EGVPFVYGGQ ESLRTKGGDE NSYKSPDAVN QIDWDRVQDN QELVDYFKQL
     VQLRKDESAF RLTNYADIDK TVKVLQDGKN GVFAFEYLAG GHKLYVLFNV NDSAQVFDAV
     NLTNGRVLLG SDAVTLGTVT NLAALSTLVV REDLPQTVTI NYQDDNGQLV KTTTVTLTAA
     GTAYTLTAPA GYHLTGDQTT VSYDFDNDGT ARIVTVLVAK MTTDNGQPGG QPSGGNGQTG
     DHHGKENGQT GATTQPGGGS TTTTAEDQRA GEVEKPTIPT TTANQATSSA TKATLTPTTA
     AKAGRAAATG LPQTGERAGQ SASLLGLLGI MLAGLMSLVK PQRKRN
//
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