ID A0A0C1YF87_9ACTN Unreviewed; 460 AA.
AC A0A0C1YF87;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Protease {ECO:0000313|EMBL:KIF79322.1};
GN ORFNames=QR77_31275 {ECO:0000313|EMBL:KIF79322.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF79322.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF79322.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF79322.1,
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:KIF79322.1}.
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DR EMBL; JTHL01000001; KIF79322.1; -; Genomic_DNA.
DR RefSeq; WP_040028953.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C1YF87; -.
DR STRING; 1576605.QR77_31275; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000031584; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF224; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KIF79322.1};
KW Protease {ECO:0000313|EMBL:KIF79322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT DOMAIN 34..165
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 185..373
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 48519 MW; A9F17F80FCF4708F CRC64;
MDLHPQPTAG EARPWAFPAP ERGALDNGMT VLRCHRPGQQ VVAVEISLAA PLDAEPEGLD
GIATIMVRAF SEGTDKHSAE EFAAELERCG ATLDAAADHP GVRVSLEVPV SRLPKGLGLL
AEALRAPAFL ESEIERLVNN RLDEIPHESA NPARRAAKQL SKELFPASLR MSRPRQGTAE
TVARIDAAGV RAFYDAHVRP ATATAVVVGD LTDVDLDTLL AETLGTWTGN MAAARPVPPI
TADDTGRVVI VDRPGAVQTQ LLIGRIGADR HDRVWPAQVL GTYCLGGTLT SRLDRVLREE
KGYTYGVRAY GQVIRSSDPA TPGGPTGAAM LAISGSVDTE STGPALDDLW KVLRTLAAEG
LTDAERDVAV QNLVGVAPLK YETAASVADT LADQVEQHLP DDFQAQLYAR LAETGTVEAT
AAAVNAFPVD RLVTVLVGDA AQIKDAVTAL GIGEVTVVTG
//