ID A0A014NPN1_9GAMM Unreviewed; 508 AA.
AC A0A014NPN1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=pectate lyase {ECO:0000256|ARBA:ARBA00012272};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN ORFNames=BG55_09030 {ECO:0000313|EMBL:EXU75760.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75760.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75760.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75760.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU75760.1}.
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DR EMBL; JFHN01000044; EXU75760.1; -; Genomic_DNA.
DR RefSeq; WP_034936490.1; NZ_JFHN01000044.1.
DR AlphaFoldDB; A0A014NPN1; -.
DR STRING; 69222.BG55_09030; -.
DR PATRIC; fig|69222.5.peg.1863; -.
DR OrthoDB; 4298856at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000019918}.
FT REGION 11..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 49728 MW; 8E500406D0B6FD4F CRC64;
MSGLTLSITI PNSLGHFQPG ENNGLSTGNN TNSSLGQQPF DQQTIEQMAQ LLAELLKPLL
TSQSGDSSSD ANGTSPISGL GNTGGTSGAS GNSLLSGLGG AGGLSGQNGS VSGTSQDDSQ
STLNDMSSNG LDQSLSSDGQ GGGNISDNPL LKALLKLIAQ MMDGLNGQFG QPDGSDDSSS
SGGGTSGADG SGGGGSGGSS PFSGTSLADG SGGGSSLGGG SLSGGGSPFG GGSLTGGAGG
GSSLGGGSSL GGGFSPSTSP VSSGQGGTSL LSGNPAVGST THTPVSDQAD PLGSAGTGAA
QDVGFPTASA NPNVVHDTIV VKAGQVFDGK GQTFTAGKEL GDGTQSESQK PLFKLEDGAS
LKNVVIGDNG ADGIHLYGDA KIDNLHVTNV GEDAITVKAN KEGKKSNVEI SNSTFQNASD
KILQLNADTD LTVNNVKAKD FGTFVRTNGG QQGDWDLNLS HISAQNGKFS FVKSDSEGLK
VNTSDVSLDN VENHYKVPAS AKLTAVAS
//
