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Database: UniProt
Entry: A0A1E8CYU0_9MICO
LinkDB: A0A1E8CYU0_9MICO
Original site: A0A1E8CYU0_9MICO 
ID   A0A1E8CYU0_9MICO        Unreviewed;       407 AA.
AC   A0A1E8CYU0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase M50 {ECO:0000313|EMBL:OFE17574.1};
GN   ORFNames=BA895_15095 {ECO:0000313|EMBL:OFE17574.1};
OS   Humibacillus sp. DSM 29435.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Humibacillus.
OX   NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE17574.1, ECO:0000313|Proteomes:UP000175826};
RN   [1] {ECO:0000313|Proteomes:UP000175826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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}.
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:OFE17574.1}.
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DR   EMBL; MAST01000006; OFE17574.1; -; Genomic_DNA.
DR   RefSeq; WP_070190903.1; NZ_MAST01000006.1.
DR   AlphaFoldDB; A0A1E8CYU0; -.
DR   STRING; 1869167.BA895_15095; -.
DR   OrthoDB; 9781963at2; -.
DR   Proteomes; UP000175826; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175826};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..192
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   407 AA;  41838 MW;  1DD654A36692DCCB CRC64;
     MSEGGHADRA DQAGRAGNGY GWRIGAVGGT PVYIARSWPL IIVLLLLVVS PTLRSSGRSM
     GFAVFVAASS GVLLLVSVLV HEAAHAVVAG LRGHQVDRVV ADVWGGHTVY DSTDVTPGTT
     ALVAVVGPLS NLALALVAWL AQPLVSNDLA ANLLGATAYV NLFVGLFNLL PGLPLDGGQI
     VSSLVWQVTG RKGTGLSAAG WLGRVVAVGA VLWFIGVPLL RGQQPSLISL VWVAMIAFFL
     WRGASASIRS GQIHDATAGP ALSVLEPVVL VAGDMTVAAA ANLMVGAPSF STETEGGPAA
     APRGAWVAVT DSGGWPFGLV DPAAAAAVPV VSRHTARLSA VALAQPRAWV LELPPDAVLT
     ELVRLMSERS LSVAIVVDAQ TRRVAGLATA QHINDVVGAE LARRGRR
//
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