ID L0DBN0_SINAD Unreviewed; 268 AA.
AC L0DBN0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Zn-dependent protease {ECO:0000313|EMBL:AGA26260.1};
GN OrderedLocusNames=Sinac_1898 {ECO:0000313|EMBL:AGA26260.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA26260.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA26260.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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; CP003364; AGA26260.1; -; Genomic_DNA.
DR RefSeq; WP_015245427.1; NZ_JH621477.1.
DR AlphaFoldDB; L0DBN0; -.
DR STRING; 886293.Sinac_1898; -.
DR KEGG; saci:Sinac_1898; -.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_080388_0_0_0; -.
DR OrthoDB; 9800627at2; -.
DR Proteomes; UP000010798; Chromosome.
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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AGA26260.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:AGA26260.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..182
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 268 AA; 28764 MW; 1A0DD2E319780045 CRC64;
MQSSWKLGRW AGIDVYLHST FMLILAYAGM VLGGFPAILL VVAAFSCVLL HEFGHALMAR
RFGIETEDIT LYPIGGVARL RRMPKSPGAE MAIALAGPAV NVVIAAILAL VLGLGLFDGP
GTPVILGAFA MNLLSINIVL VLFNMIPAFP MDGGRVLRAA LSGWLGRVRA TMIAASIGRG
LATLFGLYSL VHGDWFQVIL AMFIYVVAGA ELRQVLAEGR SDSDSDSHNG SDDVWVAPPG
FRWVSRGKGV WQLAPIVVHT SNRPSPWR
//
