ID A8E417_PSEVI Unreviewed; 562 AA.
AC A8E417;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Harpin HrpZ {ECO:0000256|ARBA:ARBA00018764};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN Name=hrpW {ECO:0000313|EMBL:AAX58449.1};
GN ORFNames=PAI-R2-ORF24 {ECO:0000313|EMBL:AAX58449.1};
OS Pseudomonas viridiflava.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=33069 {ECO:0000313|EMBL:AAX58449.1};
RN [1] {ECO:0000313|EMBL:AAX58449.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BOR1.3d {ECO:0000313|EMBL:AAX58449.1};
RX PubMed=17720907; DOI=10.1534/genetics.107.077925;
RA Araki H., Innan H., Kreitman M., Bergelson J.;
RT "Molecular evolution of pathogenicity-island genes in Pseudomonas
RT viridiflava.";
RL Genetics 177:1031-1041(2007).
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 -!- SUBUNIT: Homomultimeric. {ECO:0000256|ARBA:ARBA00011397}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Host cell membrane {ECO:0000256|ARBA:ARBA00004165}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the harpin HrpZ family.
CC {ECO:0000256|ARBA:ARBA00009821}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463}.
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DR EMBL; AY859276; AAX58449.1; -; Genomic_DNA.
DR AlphaFoldDB; A8E417; -.
DR CAZy; PL3; Polysaccharide Lyase Family 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0034053; P:symbiont-mediated perturbation of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR006961; HrpN/Z.
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; PF04877; Harpin; 1.
DR Pfam; PF03211; Pectate_lyase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hypersensitive response elicitation {ECO:0000256|ARBA:ARBA00022978};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00022870};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transport {ECO:0000256|ARBA:ARBA00023065};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT REGION 61..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 52942 MW; BB3A78A3721668FD CRC64;
MSDLTSLSGS MGNLSSLPGV GGTSMGIGAS LTGAGQGAQG GQSALQELAG MLAEMLLGSG
SGSGSGSGAG GGQSAGKGAQ GGQSDLDSLL QSLQGNGQNG DRQTKDSGTA GGGEKELLTQ
VLMALFEKIL GGSDSSSGAG NGSGGGSGGA SGIGGGGTGA SKDAGALGQG QGLGGTQGAA
GGSSTEDLVN TLMQKLGGGS LDNSIQPTAD GGGEMSQNGK LKELLEMIAQ FMDSHPETFS
QPSDGASKGG GGGGGGGGVA PTGTGGGGGA PSVGGGGGGG GGSPSVGGSG GGGGGGGTPS
LGGGGGTPSI GGGGSTPAPT PGAGGGTPTP TGPTGTPSPT GPTGTGTSGS ATPVSFPTAS
SNPTVINETI KVGPGETFDG GGKTFTAGKA LGDGGQGEGQ KPMFELAEGA TLKNVVLGDN
AADGVHVRAA SEKAVNVDNV HWTNVGEDAL TVKGEGGAKV TNLNITNSSA QGANDKVFQL
NADANVNVDN FKVKDFGTFM RTNGGQQGDW NLDLKNISAE NGKFSFVKSD SEGLNLSTSG
IDLKNVENAY SKLPGSTNHK EA
//
