ID   PEL2_BACIU              Reviewed;         345 AA.
AC   P94449;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Pectin lyase;
DE            Short=PNL;
DE            EC=4.2.2.10;
DE   AltName: Full=Endo-pectin transeliminase;
DE   AltName: Full=Protopectinase-R;
DE            Short=PPase-R;
DE   Flags: Precursor;
GN   Name=pelB; Synonyms=ppr;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231;
RX   PubMed=8977121; DOI=10.1016/s0014-5793(96)01257-4;
RA   Sakamoto T., Kawasaki H., Sakai T.;
RT   "Molecular cloning and nucleotide sequence of the gene encoding phosphate-
RT   inducible pectin lyase of Bacillus subtilis.";
RL   FEBS Lett. 398:269-273(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-49, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, ACTIVITY REGULATION, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231;
RX   PubMed=7764545; DOI=10.1271/bbb.58.353;
RA   Sakamoto T., Hours R.A., Sakai T.;
RT   "Purification, characterization, and production of two pectic
RT   transeliminases with protopectinase activity from Bacillus subtilis.";
RL   Biosci. Biotechnol. Biochem. 58:353-358(1994).
CC   -!- FUNCTION: Catalyzes the depolymerization of pectins of methyl
CC       esterification degree from 13 to 75%, with an endo mode of action.
CC       Cannot degrade polygalacturonate. Also displays protopectinase
CC       activity, i.e. releases pectin from protopectin.
CC       {ECO:0000269|PubMed:7764545}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC         Evidence={ECO:0000269|PubMed:7764545, ECO:0000269|PubMed:8977121};
CC   -!- ACTIVITY REGULATION: Inhibited by Hg(2+) and Mn(2+). Not affected by
CC       EDTA in vitro. {ECO:0000269|PubMed:7764545}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Retains 70% of activity after 16 hours incubation
CC         in the pH range 4-11, at 37 degrees Celsius.;
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Retains more than 90% and
CC         70% of activity after 30 min incubation at pH 6 at 50 and 60 degrees
CC         Celsius, respectively.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7764545}.
CC   -!- INDUCTION: Up-regulated under high-phosphate conditions.
CC       {ECO:0000269|PubMed:7764545, ECO:0000269|PubMed:8977121}.
CC   -!- MISCELLANEOUS: Does not require calcium for activity.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; D83791; BAA12119.1; -; Genomic_DNA.
DR   RefSeq; WP_003220382.1; NZ_ML241275.1.
DR   AlphaFoldDB; P94449; -.
DR   SMR; P94449; -.
DR   STRING; 483913.AN935_09735; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   GeneID; 64303818; -.
DR   PATRIC; fig|1423.172.peg.39; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0047490; F:pectin lyase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:7764545"
FT   CHAIN           25..345
FT                   /note="Pectin lyase"
FT                   /id="PRO_0000367324"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   345 AA;  37996 MW;  A18B5C47E438E7E7 CRC64;
     MKRFCLWFAV FSLLLVLLPG KAFGAVDFPN TSTNGLLGFA GNAKNEKGIS KASTTGGKNG
     QIVYIQSVND LKTHLGGSTP KILVLQNDIS ASSKTTVTIG SNKTLVGSYA KKTLKNIYLT
     TSSASGNVIF QNLTFEHSPQ INGNNDIQLY LDSGINYWID HVTFSGHSYS ASGSDLDKLL
     YVGKSADYIT ISNSKFANHK YGLILGYPDD SQHQYDGYPH MTIANNYFEN LYVRGPGLMR
     YGYFHVKNNY SNNFNQAITI ATKAKIYSEY NYFGKGSEKG GILDDKGTGY FKDTGSYPSL
     NKQTSPLTSW NPGSNYSYRV QTPQYTKDFV TKYAGSQSTT LVFGY