GenomeNet

Database: UniProt
Entry: A0A317L3A9_9BACI
LinkDB: A0A317L3A9_9BACI
Original site: A0A317L3A9_9BACI 
ID   A0A317L3A9_9BACI        Unreviewed;       369 AA.
AC   A0A317L3A9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
GN   ORFNames=DLJ74_00235 {ECO:0000313|EMBL:PWU70307.1};
OS   Gracilibacillus dipsosauri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=178340 {ECO:0000313|EMBL:PWU70307.1, ECO:0000313|Proteomes:UP000245624};
RN   [1] {ECO:0000313|EMBL:PWU70307.1, ECO:0000313|Proteomes:UP000245624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD1 {ECO:0000313|EMBL:PWU70307.1,
RC   ECO:0000313|Proteomes:UP000245624};
RA   Deutch C.E., Yang S.;
RT   "Genomic analysis of Gracilibacillus dipsosauri DD1 reveals novel features
RT   of a salt-tolerant amylase.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC       pectins of methyl esterification degree from 22 to 89%, with an endo
CC       mode of action. In contrast to the majority of pectate lyases, displays
CC       high activity on highly methylated pectins.
CC       {ECO:0000256|RuleBase:RU367009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000695,
CC         ECO:0000256|RuleBase:RU367009};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913,
CC         ECO:0000256|RuleBase:RU367009};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367009}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000256|ARBA:ARBA00006463, ECO:0000256|RuleBase:RU367009}.
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:PWU70307.1}.
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; QGTD01000001; PWU70307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317L3A9; -.
DR   OrthoDB; 148600at2; -.
DR   Proteomes; UP000245624; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR   PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 2.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU367009};
KW   Lyase {ECO:0000256|RuleBase:RU367009, ECO:0000313|EMBL:PWU70307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245624};
KW   Secreted {ECO:0000256|RuleBase:RU367009};
KW   Signal {ECO:0000256|RuleBase:RU367009}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|RuleBase:RU367009"
FT   CHAIN           27..369
FT                   /note="Pectate lyase"
FT                   /evidence="ECO:0000256|RuleBase:RU367009"
FT                   /id="PRO_5025086368"
FT   DOMAIN          32..169
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   369 AA;  40798 MW;  4AB45478912870FE CRC64;
     MRAKLLTMLA FALLLVGAIS VESLEAASFD SSKSYKIINR FSGKALEVYE WSTSDGGNIV
     QYDDLGGLNQ QWRIINVGEG YHKIVNQNSI KAMEVYDWST EDGANVSQWY DWNAANQQWA
     IEGIGNGYVK IVNRHSGKAL EVFDWSTENG ANVVQWDDWG GESQQWRIIE VPPSDTITVN
     QTIVVESGEV FDGEGKRYVA NPDTVGDGSQ GEDQDPVFRL EDGATLKNVV IGHPAADGVH
     TYGDVLVQNV VWEDIGEDAL TIKDDGHVTI RGGMAQKGSD KMFQVNAPST FEIINFTADD
     AGKMIRQNGG TTFKTSIFID GSVITNMDEA IFRTDSDSSE VTMTNTRYSD VGRKWYNVEN
     VSESGNYEY
//
DBGET integrated database retrieval system