ID H6CET4_9BACL Unreviewed; 230 AA.
AC H6CET4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=WG8_0948 {ECO:0000313|EMBL:EHS59070.1};
OS Paenibacillus sp. Aloe-11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS59070.1, ECO:0000313|Proteomes:UP000005078};
RN [1] {ECO:0000313|Proteomes:UP000005078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aloe-11 {ECO:0000313|Proteomes:UP000005078};
RX PubMed=22461553; DOI=10.1128/jb.00087-12;
RA Li N.Z., Xia T., Xu Y.L., Qiu R.R., Xiang H., He D., Peng Y.Y.;
RT "Genome Sequence of Paenibacillus sp. Strain Aloe-11, an Endophytic
RT Bacterium with Broad Antimicrobial Activity and Intestinal Colonization
RT Ability.";
RL J. Bacteriol. 194:2117-2118(2012).
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; JH601047; EHS59070.1; -; Genomic_DNA.
DR RefSeq; WP_007428938.1; NZ_JH601047.1.
DR AlphaFoldDB; H6CET4; -.
DR HOGENOM; CLU_044863_3_1_9; -.
DR Proteomes; UP000005078; 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 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, ECO:0000313|EMBL:EHS59070.1};
KW Secreted {ECO:0000256|RuleBase:RU367009};
KW Signal {ECO:0000256|RuleBase:RU367009}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT CHAIN 34..230
FT /note="Pectate lyase"
FT /evidence="ECO:0000256|RuleBase:RU367009"
FT /id="PRO_5025090751"
SQ SEQUENCE 230 AA; 24626 MW; 8F551C9886F970B5 CRC64;
MNTKTAKVLK KGMSIALSGM LVALFVGNYS AHAAPEVVHK TIVVKAGEVY DGKGKTVVAD
PDTLGDGSQK ENQKPIFKLE NNATLKNVII AAPAADGVHV YGNGTISNVT WEDVGEDALT
LKKSGTVNIT GGGAFHAYDK VFQMNAEGTI NIKNFRADDI GKLARQNGGT KYKVNMTLDN
SDISNVKDSI FRTDSSSSSA RITNSRFHNV EQLFKGFKSS NTSESGNTKY
//
