ID A0A432MHD1_9BACT Unreviewed; 272 AA.
AC A0A432MHD1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Zn-dependent protease {ECO:0000313|EMBL:RUL86708.1};
GN ORFNames=TsocGM_15465 {ECO:0000313|EMBL:RUL86708.1};
OS Tautonia sociabilis.
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Tautonia.
OX NCBI_TaxID=2080755 {ECO:0000313|EMBL:RUL86708.1, ECO:0000313|Proteomes:UP000280296};
RN [1] {ECO:0000313|EMBL:RUL86708.1, ECO:0000313|Proteomes:UP000280296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM2012 {ECO:0000313|EMBL:RUL86708.1,
RC ECO:0000313|Proteomes:UP000280296};
RA Toschakov S.V.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RUL86708.1, ECO:0000313|Proteomes:UP000280296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM2012 {ECO:0000313|EMBL:RUL86708.1,
RC ECO:0000313|Proteomes:UP000280296};
RA Kovaleva O.L., Elcheninov A.G., Van Heerden E., Toshchakov S.V.,
RA Novikov A., Bonch-Osmolovskaya E.A., Kublanov I.V.;
RT "Tautonia sociabilis, a novel thermotolerant planctomycete of
RT Isosphaeraceae family, isolated from a 4000 m deep subterranean habitat.";
RL Submitted (JAN-2019) 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:RUL86708.1}.
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DR EMBL; RYZH01000030; RUL86708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432MHD1; -.
DR OrthoDB; 9800627at2; -.
DR Proteomes; UP000280296; 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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RUL86708.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:RUL86708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280296};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..115
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 121..185
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 272 AA; 28708 MW; 003929E763F4C92E CRC64;
MRLSWKLGRV AGIDLYVHAT FFVMMAVLAT AQRGVEAVLM VLALFGCVLL HELGHALTAR
RFGIPTEHIT LYPIGGVARL HRMPREPGAE LLIALAGPAV NVGIAATLFA GLAVVSALAP
AMAAGSIGMV LGDLLRVNLL LACFNLLPIF PMDGGRVLRA MLSRPLGRLR ATEIAAALGQ
ALAMIAGGAC VVAIVVTGQP LFLLHLALAA FIFLAAGGER GQVRAEELRL RASQAAPGYT
WIDLGNGVWQ LAPVILLDEP APRPFRGARP WL
//