ID M1QXL5_BACTU Unreviewed; 549 AA.
AC M1QXL5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Microbial collagenase {ECO:0000313|EMBL:AGG04954.1};
DE EC=3.4.24.3 {ECO:0000313|EMBL:AGG04954.1};
GN ORFNames=H175_233p100 {ECO:0000313|EMBL:AGG04954.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OG Plasmid pIS56-233 {ECO:0000313|EMBL:AGG04954.1,
OG ECO:0000313|Proteomes:UP000011719}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG04954.1, ECO:0000313|Proteomes:UP000011719};
RN [1] {ECO:0000313|EMBL:AGG04954.1, ECO:0000313|Proteomes:UP000011719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGG04954.1};
RC PLASMID=Plasmid pIS56-233 {ECO:0000313|Proteomes:UP000011719};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP004135; AGG04954.1; -; Genomic_DNA.
DR RefSeq; WP_000688777.1; NC_020394.1.
DR AlphaFoldDB; M1QXL5; -.
DR GeneID; 67470330; -.
DR KEGG; btht:H175_233p100; -.
DR PATRIC; fig|1286404.3.peg.6251; -.
DR HOGENOM; CLU_027782_1_0_9; -.
DR Proteomes; UP000011719; Plasmid pIS56-233.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04843; Peptidases_S8_11; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034073; Subtilisin_DY-like_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGG04954.1};
KW Plasmid {ECO:0000313|EMBL:AGG04954.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 237..481
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 505..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 59705 MW; 0B542DF5936D2070 CRC64;
MKIFKGILVS SIALTAFNGV GGLLPSEKSE VAYAATYNYS NKQLNSTVHK QVTKQLILKF
KNEANLPYQD GIEKFIKEEK QDPELIGILA EYPNVTINRL FNSLNPKEIK NLGKEIKDSD
HISSNLLNYY IVETQDDIDV QALLTKIEKS SLVETAYLQE EEAPPAERLP NLSVNPYDEP
RLTRQGYLEP APLGINAPYA WSIKGGDGKG TTFVDMEYGW LFSHEDLVNQ KIELISGQNK
SEHHDHGTSV LGIVSAEDNN IGGIGIAPKA KVKVVSQIRD NGNYNTADAI LSAVNNMQAG
DILLLEAQAT YDGYGDKNYF PVEVKPDIFD AIRMGTNKGI IIIEAGANGG NDLDQFRDRN
GKQVLNRNSP DFKDSGAIMV GAASARVPHK RSYFSNYGSR VDVYGWGNAV DTTDAKPSEF
ITNLYTSSFA GTSSASPIIA GAAASIQGIV KNNQGRVYTP RQLRAILSDS STGTKSNDPT
SDKIGVLPDL KAILSKLGFS PNLSNDSSIA FPEEQEINKG NKGNEGSTIT FPKEDSANGE
GDSSFIFPE
//
