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Database: UniProt
Entry: Q82ND7_STRAW
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ID   Q82ND7_STRAW            Unreviewed;       950 AA.
AC   Q82ND7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Metalloprotease, secreted {ECO:0000313|EMBL:BAC69076.1};
GN   ORFNames=SAVERM_1366 {ECO:0000313|EMBL:BAC69076.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC69076.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC69076.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC69076.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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DR   EMBL; BA000030; BAC69076.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q82ND7; -.
DR   KEGG; sma:SAVERM_1366; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_314212_0_0_11; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:BAC69076.1}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          112..142
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          290..451
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          455..609
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          266..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        536
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   950 AA;  99568 MW;  80ECD1A01C877E9F CRC64;
     MGQSRADSKR PTGLSRARRS GISGAAALIG VAALVVSAVP ADAKAGGPVP PPSPGELIPG
     QKTATPALVE GLREQAPAAR NAAGAARAYL AAKQDRYRIA DPGRDLEPLG TVTADGQETV
     RLRQRYHGIP VLGGQYVVRM EKQDGGRVVT GTSGKYFTGL RTGTTAEVDD ALAVERAVDA
     VLARLGAEKF TAYGEDDEGK KDATPLTGTS HGLVVLPTGT GVLARHVTVR GADPARGEPV
     LREVYVDAQA GYPVLQYSGI RTFDAPGTTA EGSAASHPAQ EPTEPAPGET GSGVKLDGKP
     VELQVTHDDT RAAYVLRDHS RIHNDTADVL ATWDARGKWA SDVVGNWPAD LQEFASPTPA
     FGAEATEAGA VDAHWAAGQV YDYYKNKHGR DSLDGRGMSI NSLVGTTDYG QPYVNAFWDG
     QKMVYGNGDA EYRPLAAGLD VVGHEMTHGV VDHSADLVYA GQSGAMNEAI ADYFGNAIET
     DVHGIAMADP DSGLLGEALC RTRTPRECAV RDLNDGRTTA KSFLGVGFGT DNGGVHLNST
     IFSGALWDIR EDVGPTLADK IVYKALTEYL TPLDGFTQGR DAVIAAARAL GTGGKDLTAV
     QRAFNAHGIV PNWELALGVD SDLLIERVNT YDSQLGAGGD WWTAATSNEE GSEAYSVWAG
     RTDGTGQLKL MSPNDGRYHV NPATDGKTVV WQAHGTSGVD ILARPLAGGP VKTLWHGRSV
     GGALDVDGDV VAFAYNNHGG RAGVAYLSLK DPANVVTIGG GTYHRATFPS LSHGKVVYQD
     RQRVSAVYET TTRVVDVATG EDKVIQRAAP GASLGPTAVT GDHVYWLLDE IDQNGTTALR
     RAGLDGSGIT DLSPETGPES LNVFDLTASE GAVTVDARTP DPAFRNESLA KLWQFSAEGK
     GDGVRKSRVS CNRGEQLSAA AASGTQVVWL DATTGISNVV TRTRPSGTCG
//
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