ID A0A0C2B9C8_9ACTN Unreviewed; 395 AA.
AC A0A0C2B9C8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KIF74661.1};
GN ORFNames=QR77_13160 {ECO:0000313|EMBL:KIF74661.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF74661.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF74661.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF74661.1,
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 -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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:KIF74661.1}.
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DR EMBL; JTHL01000001; KIF74661.1; -; Genomic_DNA.
DR RefSeq; WP_040021860.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2B9C8; -.
DR STRING; 1576605.QR77_13160; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000031584; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 98..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 395 AA; 40213 MW; 4915E983F76DE812 CRC64;
MSGSELHHSP RAFRRGATLT FVFASVLATA AATNSLPGEA HRTRHAATRS VASTVDAALV
AKAAAEAMAD GKSGTEAAEE VVSRSGDRWG AVYDKGEYEE FEQALDGTYT GVGLWARRTA
EGLVEVTRVQ PGGPAARAGV RAGDTVTDID GSSVAKRPVT EVMGMLRGDS RGPGAPAGGA
AGSSVTVSLD RAGHHWTEHL RRAELSTESV TVGTLTGGAR LIKVDSFTKG TGERVKEAVR
SAPKGAGVLL DLRGNGGGLV AEAVTAASAF LDGGLVATYD IKGEQRALYA SGGGDTGRPL
VVLVDSGTMS AAELLTGALQ DRGRAVTVGA RTFGKGSVQM PSKLPDGSVA ELTVGHYRTP
SGHAVDGRGI TPDVAVTDRA QQRAETVLSG LGGTA
//
