ID C9ZC44_STRSW Unreviewed; 602 AA.
AC C9ZC44;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative protease {ECO:0000313|EMBL:CBG71734.1};
GN OrderedLocusNames=SCAB_46811 {ECO:0000313|EMBL:CBG71734.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG71734.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG71734.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG71734.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN554889; CBG71734.1; -; Genomic_DNA.
DR RefSeq; WP_013002328.1; NC_013929.1.
DR AlphaFoldDB; C9ZC44; -.
DR STRING; 680198.SCAB_46811; -.
DR GeneID; 24310522; -.
DR KEGG; scb:SCAB_46811; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_8_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CBG71734.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CBG71734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 506..595
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 59105 MW; A0F4BAF70F39BF32 CRC64;
MSTENEGTPV PPAPSAPPVP VDTAAASAQT PAHEPSEAPA ESPAEPAGGT SADNAPTTQL
PPVPPTAPEP AATAVQPQVP HVPQAERPVA PHPTAEQPVM QHPTGQHPTA QYPTAQYPTD
QQPMAHQPHP ELVSAGAPAY AAAPGQGHGM GQASGGGYGH APGGTGSSAP DASWPPPVPP
AVPSYADNGG GAYADTGAAG GAGGTGGPGD GGWGSSWQHT QQPAPKPAGR KRGGLIAAVL
VAALVAGGVG GGIGYTLADR NDNSTGSTTV SASQNGGDVK RAAGTVAAVA SSALPSTVTI
EASNSDGDGG TGTGFVFDRE GHIVTNNHVV AEAVDGGKVS ATFPDGKKYA AEVVGHAQGY
DVAVIKLKNA PSNLQPLTLG DSDKVAVGDS TIAIGAPFGL SNTVTTGIIS AKNRPVASSD
GSSGSKASYM SALQTDASIN PGNSGGPLLD ARGNVIGINS AIQSASSGGS FGSGQAGSIG
LGFAIPINQA KNVAQQLIRT GKPVYPVIGA SVSLEEGTGG AKITNSGGGG SESITANGPA
DKAGLKPGDV ITKLDDHVID SGPTLIGEIW THRPGDKVTL TYTRDGKTRT ADVTLGEREG
DS
//
