ID A0A2K8PP42_STRLA Unreviewed; 670 AA.
AC A0A2K8PP42;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ricin-type beta-trefoil lectin domain protein {ECO:0000313|EMBL:ATZ28501.1};
GN ORFNames=SLAV_33650 {ECO:0000313|EMBL:ATZ28501.1}, SLLC_31820
GN {ECO:0000313|EMBL:QUQ58326.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ28501.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ28501.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ28501.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ58326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ58326.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP024985; ATZ28501.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ58326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8PP42; -.
DR KEGG; slx:SLAV_33650; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Lectin {ECO:0000313|EMBL:ATZ28501.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000231791};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..670
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039565661"
FT DOMAIN 532..667
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 26..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 69012 MW; 33E8DFFF33DD23A9 CRC64;
MLLTAAMATA AVIAGGLAYA GLDPDAEATT PAQASGAGAP AEPAAAPARD AEPAALSSAP
ANENARGMVY DGLKAAPKGD RCVGVYRTDA GLCTHGPDAP PGGVDIKKDV QPVVRTKAPA
ADPAAPASAD PAATEGGGRP QDAPAADART AASKAAPAPP ASGSQGIAAG PAGQTVQCDG
DGTSGNRVQV VYAHGPGRDR YAEYLASFRK WAADADLIYA ASAKETGGIR HIRYVTAADC
TPSVISIELP DSALAEFSAT NAALAGKGLD RRDRKYMIFA DTQIYCGIGT FNGDERPGQN
NLSNFGPSYG RTDSGCWGGH TAAHELGHNL GAVNNSAPNT SRGAHCTDEF DVMCYSDTPY
YPQMRNVCTN QASENILDCN HDDYFHTSPK PGSYLATHWN IADNQFLMRT DGGGTGPGPN
PNPGPTAKPT PSPSPTKKPT GGGPVVTAGQ IQADSVVLSW PRTEGAAWYQ VLLNGKHLTW
VQSTSLRVYG LRAGTDYTAA VSVRDTAGRD SGPGKATSFR TTATGGGATT PGTRYVLGNG
SSGMAAEMWD GRTADGTVLV AGRTNGYAQQ QWYFDDAGSG LVRIRSAVSG KCLQPGGAPA
AGMWVSQQPC GNSASQQWRL TTRDGSTTVS DPSGGFALAV SNRPYYGNWL LELQRADGRP
AQAWTARKAG
//
