ID   L7PID0_9XANT            Unreviewed;       369 AA.
AC   L7PID0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   Name=hrpW {ECO:0000313|EMBL:AFV80107.1};
OS   Xanthomonas arboricola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=56448 {ECO:0000313|EMBL:AFV80107.1};
RN   [1] {ECO:0000313|EMBL:AFV80107.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 19146 {ECO:0000313|EMBL:AFV80107.1};
RA   Vandroemme J.;
RL   Submitted (JAN-2012) 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}.
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DR   EMBL; JQ595993; AFV80107.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7PID0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR   PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU367009};
KW   Lyase {ECO:0000256|RuleBase:RU367009};
KW   Secreted {ECO:0000256|RuleBase:RU367009}.
FT   REGION          46..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..73
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  37371 MW;  F97216EBD9CD6C93 CRC64;
     MNLAIPSHTT ASLQPSSFSL SQQQALTAVI MSMLAYCMQR MLSDMLQPQD QPSSDGQPPT
     NPTPTPSLPP SNPPGSSNAG GQHGSGTGDG SGSNGGNNKG SGSTSGTAAG NGASPTSPGQ
     PATPPGSGQP VTPGPSGTQA PLPPGKVVTA PPGVQNKPIV VHKGEVFDGK NQLYVGGPCL
     GKGNQDEHQQ PLFVVEDGGS LCNVNMTGGG DGVHFMGSGK MVNCVNEDVS EDAVTIDGQG
     NREHDAGIAG CSPEVSGRPK VEIINCTFKN AADKVVQDNG AADVVMSGDT VEGASKVFRT
     NGGHTDIDTN LQVENCEFNQ VKEAVFRTDA PGATVKLANL KTDAPNEVIA PDASQAIGAT
     RIGYKAYSG
//