ID A0A0S6W124_9BACT Unreviewed; 240 AA.
AC A0A0S6W124;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M50 domain-containing protein {ECO:0000259|Pfam:PF02163};
GN ORFNames=U14_04728 {ECO:0000313|EMBL:GAK53463.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK53463.1};
RN [1] {ECO:0000313|EMBL:GAK53463.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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DR EMBL; DF820459; GAK53463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6W124; -.
DR STRING; 1499966.U14_04728; -.
DR HOGENOM; CLU_086979_0_0_0; -.
DR Proteomes; UP000030700; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06158; S2P-M50_like_1; 1.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR044537; S2P-M50-like.
DR PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..194
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 240 AA; 27088 MW; 020DA63D974A5550 CRC64;
MLFELNPLHL AEGLVWYIVF LFSTVCHEAA HAFASLKLAD RTAHEGGQVT LDPLPHIRRE
PIGMVVIPIV SFLMSGWMMG WASAPYDPAW AMRYPRRSAL MALAGPSANF VLFAIAFLMI
RAGVAFEWFY APDSITFSQV TVAVAAKGVS VAVAKFLSIL FSLNLILCVF NLLPLPPLDG
SSIFPLFLER RMGQEYLDFL HRNRSFAFFG LYVAWQFFHV IFNPIHLFVL NLLYPGLQYH
//
