ID   PEL1_BACSU              Reviewed;         345 AA.
AC   O34819; Q796F4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Pectin lyase;
DE            Short=PNL;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelB; OrderedLocusNames=BSU18650;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF027868; AAB84422.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13757.1; -; Genomic_DNA.
DR   PIR; E69674; E69674.
DR   RefSeq; NP_389746.1; NC_000964.3.
DR   RefSeq; WP_009967389.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34819; -.
DR   SMR; O34819; -.
DR   STRING; 224308.BSU18650; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; O34819; -.
DR   PRIDE; O34819; -.
DR   EnsemblBacteria; CAB13757; CAB13757; BSU_18650.
DR   GeneID; 940111; -.
DR   KEGG; bsu:BSU18650; -.
DR   PATRIC; fig|224308.179.peg.2033; -.
DR   eggNOG; COG3866; Bacteria.
DR   InParanoid; O34819; -.
DR   OMA; NYWIDHV; -.
DR   PhylomeDB; O34819; -.
DR   BioCyc; BSUB:BSU18650-MON; -.
DR   Proteomes; UP000001570; Chromosome.
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   3: Inferred from homology;
KW   Lyase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..345
FT                   /note="Pectin lyase"
FT                   /id="PRO_0000367323"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   345 AA;  38108 MW;  E84A968D886F5A5D CRC64;
     MKRLCLWFTV FSLFLVLLPG KALGAVDFPN TSTNGLLGFA GNAKNEKGIS KTGTTGGKNG
     QIVYIQSVND LKTHLGGSTP KILVLQNDLS ASAKTTVTIG SNKTLVGSYA KKTLKNIYLT
     TSSAFGNVIF QNLTFEHSPQ INGNNDIQLY LDSGMNYWID HVTFSGHSYN ASGSDLDKLV
     YIGKSADYIT ISNSKFANHK YGLILGYPDD SQHQYDGYPH MTIANNYFEN LYVRGPGLMR
     YGYFHVKNNY SNNFNQAITI ATKAKIYSEY NYFGKGSEKG GILDDKGTGY FKDIGSYPSL
     NKQTSPLTSW NPGSNYSYRV QTPEYTKEFV TKYAGSQSTT LVFGY