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Database: UniProt
Entry: A0A0C2B2G8_9ACTN
LinkDB: A0A0C2B2G8_9ACTN
Original site: A0A0C2B2G8_9ACTN 
ID   A0A0C2B2G8_9ACTN        Unreviewed;       370 AA.
AC   A0A0C2B2G8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Signal protein PDZ {ECO:0000313|EMBL:KIF74129.1};
GN   ORFNames=QR77_09260 {ECO:0000313|EMBL:KIF74129.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF74129.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF74129.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF74129.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KIF74129.1}.
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DR   EMBL; JTHL01000001; KIF74129.1; -; Genomic_DNA.
DR   RefSeq; WP_040020887.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C2B2G8; -.
DR   STRING; 1576605.QR77_09260; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..370
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002145807"
FT   DOMAIN          282..358
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          35..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  37032 MW;  100CE465B4ED9715 CRC64;
     MHVSRSRGRA RRPLLPLIAA ICAVALIGGC SGAATSASDR PAPDASGTAA SDTTNQAADT
     QPAPNDLQND YETVIKNVLP SVVQIDAGDA LGSGIIWDAQ GHVVTNAHVV GKRKSFKVTV
     ATREQPVTAR LVSSFPQQDL AVIKLDTVPG GLKAAKFGDT SDVAVGQIVL AMGSPLGLSS
     SVTQGIVSAV GRTVSEGSSG GGTGATIANM VQTSAAINPG NSGGALVNLN SEVIGIPTLA
     ATDPDLGGTA APGIGFAIPV SLVKNIANQI IKNGKVNDSG RAALGIEGRT VLGPDFQPAG
     VAVVSTTKNS AAAAAGIKSG DIIVKIGNTE VPTITSLTEA LASIRPGQRV KVSYLRNGAT
     KSAQVTLGRM
//
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