ID   A0A1H9J3S5_9ACTN        Unreviewed;       532 AA.
AC   A0A1H9J3S5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Zn-dependent protease (Includes SpoIVFB) {ECO:0000313|EMBL:SEQ81438.1};
GN   ORFNames=SAMN04487983_1008121 {ECO:0000313|EMBL:SEQ81438.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SEQ81438.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SEQ81438.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SEQ81438.1,
RC   ECO:0000313|Proteomes:UP000198568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931}.
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DR   EMBL; FOFF01000008; SEQ81438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9J3S5; -.
DR   STRING; 1761906.SAMN04487983_1008121; -.
DR   OrthoDB; 9781963at2; -.
DR   Proteomes; UP000198568; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR   PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SEQ81438.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:SEQ81438.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198568};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        161..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..276
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          290..342
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..151
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  55819 MW;  563B2B3CA0DF35C8 CRC64;
     MVESGGTGRP RPDNEQSAEH PATPAPPATD LARTPDTPNP DAENPTDNTD NTGGTSNTGN
     TGGTDNSGGT GSAGGNEKPA AGESQAEVQP EPEAQPKVEV KPEGAAQPKA EADPQPQPQP
     EAEPQPEAGQ AVPPTPTLPK GPPPPRPPEQ PRGGILMGRP FGVPVYVAPS WFLVAALITW
     VFGGQLDRVL PELGALRYLV SLFFAVAFYA SVLIHELAHT IAALRFKLPV RRIQLQFFGG
     VSEIEKEAET PGREFWLAFV GPLLSLALSG LFYLAMQTVE PGTVPGVLLA GLMISNLIVA
     IFNLLPGLPL DGGRMLRAVV WKITGKPMSG TVAAAWVGRA LAVSVLIGLP LLTQSGALGS
     GAEDSVGMDT VTDALLAAIL AAIIWTGAGN SLRMARLREH LPELRARTLT RRAVPVETQT
     PLSEALRRAN DAGARALVVV DAHGEPLSLV REAAIVGVPE HRRPWVAVSG LAQDLNDGMR
     ISAELAGEDL LDVLRATPAT EYLVVEETGE IFGVLSAADV ERAFVKAMAR PS
//