ID   PTLY_THESQ              Reviewed;         365 AA.
AC   B1L969;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Pectate trisaccharide-lyase {ECO:0000250|UniProtKB:Q9WYR4};
DE            EC=4.2.2.22;
DE   AltName: Full=Pectate lyase A {ECO:0000250|UniProtKB:Q9WYR4};
DE            Short=PelA {ECO:0000250|UniProtKB:Q9WYR4};
DE   Flags: Precursor;
GN   Name=pelA {ECO:0000250|UniProtKB:Q9WYR4}; OrderedLocusNames=TRQ2_0511;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC   unclassified Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1] {ECO:0000312|EMBL:ACB08867.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves unsaturated trigalacturonate from pectin. Activity is
CC       highest towards polygalacturonic acid, activity on methylated pectins
CC       decreases with an increasing degree of methylation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WYR4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eliminative cleavage of unsaturated trigalacturonate as the
CC         major product from the reducing end of polygalacturonic
CC         acid/pectate.; EC=4.2.2.22; Evidence={ECO:0000250|UniProtKB:Q9WYR4};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q9WYR4};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9WYR4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9WYR4}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000255}.
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DR   EMBL; CP000969; ACB08867.1; -; Genomic_DNA.
DR   RefSeq; WP_012310590.1; NC_010483.1.
DR   AlphaFoldDB; B1L969; -.
DR   SMR; B1L969; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   EnsemblBacteria; ACB08867; ACB08867; TRQ2_0511.
DR   KEGG; trq:TRQ2_0511; -.
DR   HOGENOM; CLU_021894_2_0_0; -.
DR   OMA; HQHVYNN; -.
DR   OrthoDB; 660314at2; -.
DR   Proteomes; UP000001687; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation; Lyase;
KW   Metal-binding; Polysaccharide degradation; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..365
FT                   /note="Pectate trisaccharide-lyase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000405017"
FT   REPEAT          149..171
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          261..287
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
SQ   SEQUENCE   365 AA;  40315 MW;  9993CF4DE4665EC3 CRC64;
     MRFSRVVSLV LLLVFTAVLT GAVKASLNDK PVGFASVPTA DLPEGTVGGL GGEIVFVRTA
     EELEKYTTAE GKYVIVVDGT IVFEPKREIK VLSDKTIVGI NDAKIVGGGL VIKDAQNVII
     RNIHFEGFYM EDDPQGKKYD FDYINAENSH HIWIDHCTFV NGNDGAVDIK KYSNYITVSW
     CKFVDHDKVS LVGSSDKEDP EQAGQAYKVT YHHNYFKNCI QRMPRIRFGM AHVFNNFYSM
     GLRTGVSGNV FPIYGVASAM GAKVHVEGNY FMGYGAVMAE AGIAFLPTRI MGPVEGYLTL
     GEGDAKNKFY YCKEPETRPV EEGKPAFDPH EYYDYTLDPV DDVPKIVVDG AGAGKLVFED
     LMSSK