ID A0A1Y4M6E6_9FIRM Unreviewed; 353 AA.
AC A0A1Y4M6E6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase M50 domain-containing protein {ECO:0000259|Pfam:PF02163};
GN ORFNames=B5F12_06005 {ECO:0000313|EMBL:OUP64383.1};
OS Pseudoflavonifractor sp. An176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=1965572 {ECO:0000313|EMBL:OUP64383.1, ECO:0000313|Proteomes:UP000196146};
RN [1] {ECO:0000313|Proteomes:UP000196146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An176 {ECO:0000313|Proteomes:UP000196146};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP64383.1}.
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DR EMBL; NFKO01000008; OUP64383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4M6E6; -.
DR Proteomes; UP000196146; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000196146};
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 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..338
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 353 AA; 39156 MW; 7C5732EAD5E9030F CRC64;
MFFILLAILI FGVMIAIHEF GHFITAKLLG IRVNEFAIGM GPALWSRTRG ETQYSLRAFP
VGGYCAMEGE DEATGDERAF SIQPAWKKII VLCAGSFMNF LMGLVIVLVL YMGVTQVRVP
VITQLADGFQ LQGESGLMVG DEILSVDGHG IWVYEDVLTF LSRNDGNGID LTVRRDGEKV
VLKDLPMERF EYQYDGQDAY GFGLIFEQVD DLSIWGRVKL ATAQTFDFVR IVWMSLGDLV
TGRVGVDQMS GVIGVVDVVS EVGTQSDSIL VGVQNVFYIM ALIAVNLAVM NMLPIPALDG
GRVLFVLLNA ISYLFFRRHI PQRLEGYIHA VVLVLLLVVM LLIAFQDVWK IVV
//
