ID A0A2S6IPL4_9ACTN Unreviewed; 483 AA.
AC A0A2S6IPL4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pectate lyase {ECO:0000313|EMBL:PPK96036.1};
GN ORFNames=CLV92_105136 {ECO:0000313|EMBL:PPK96036.1};
OS Kineococcus xinjiangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=512762 {ECO:0000313|EMBL:PPK96036.1, ECO:0000313|Proteomes:UP000239485};
RN [1] {ECO:0000313|EMBL:PPK96036.1, ECO:0000313|Proteomes:UP000239485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22857 {ECO:0000313|EMBL:PPK96036.1,
RC ECO:0000313|Proteomes:UP000239485};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|RuleBase:RU361173}.
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:PPK96036.1}.
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DR EMBL; PTJD01000005; PPK96036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6IPL4; -.
DR Proteomes; UP000239485; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR PANTHER; PTHR31683:SF187; PECTATE LYASE 18-RELATED; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00656; Amb_all; 1.
DR SMART; SM00710; PbH1; 3.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000239485};
KW Secreted {ECO:0000256|RuleBase:RU361173}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015534912"
FT DOMAIN 54..188
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 217..421
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
FT REGION 192..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 50718 MW; A24B8DF71F9DCAA0 CRC64;
MLPTTSAGTS RTTVALPAAT RTLLSTGLAV LALVAALLAV PAQRAHAATV DTDAWYVLQA
RHSGKVADVR GASTADGAPV VQWSRNDGAH QQWRFVPVGN GYYAIRARHS GKVLEVPNAL
DGAQLVQRTA STSTRQHFRL VDSADGSVRL VNRHSGKVVD VWERSTADGA ALAQYRDLDG
TNQRFALVRL GSTTTPPAQP SGPAGWAGQN GGTTGGGAAT PTRVTSASAL SAALGSSTPA
VVRVSGTITC SGMLRVRSNK TVLGEPGATI AGCGLTISGD RNVIVRNLSF RDWSDDAVNV
ESGATNVWID HNSFRNGYDG AVDVKRGADF VTVSWNRVSA HGKSMLLGHS DSNRSQDAGH
LRVTYHHNWF DGSRTRHPRV RFAQGVHVYN NYYAGNEYGV ASTMDAAVLV EGNHFEDVSE
PTLVGYADSA PGALVQRGNL FTRSGAPQSA GTVPALPYTY VLDPVNDVKS LVTAGAGAGR
ISL
//
