ID A0A1Y4WSC5_9FIRM Unreviewed; 358 AA.
AC A0A1Y4WSC5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:OUQ84708.1};
GN ORFNames=B5E42_02535 {ECO:0000313|EMBL:OUQ84708.1};
OS Flavonifractor sp. An10.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965537 {ECO:0000313|EMBL:OUQ84708.1, ECO:0000313|Proteomes:UP000196537};
RN [1] {ECO:0000313|Proteomes:UP000196537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An10 {ECO:0000313|Proteomes:UP000196537};
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:OUQ84708.1}.
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DR EMBL; NFMB01000001; OUQ84708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4WSC5; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000196537; 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 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 ECO:0000313|EMBL:OUQ84708.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OUQ84708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196537};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..343
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 358 AA; 38621 MW; 0EB2FABA05CA2569 CRC64;
MTILSIVLII LFFGVLIAVH EFGHFIAAKS LGVWVEEFAI GMGPKLFSRK KGETTYSLRA
LPIGGFCAME GEEESSDDPR SFSNKPAWKK LIILVAGAFM NFVAGLVIIV LLFAVSGVPS
LPVVNGYLAG AEDIQEQGLL PGDEFYSING HRIYFQSDAL LFLNRAGEDV AVEVVRDGQR
VDLGTLHLPY RTLTDETGQQ VLKRGITVGQ VRDMGILDTL RYGWYQAIDY VRTVWMSLGD
LISGAVGLDD MSGVIGIVAV AGQMGEQGAQ AAGLAGAFLN LLSFTALIAV NLAVMNLLPI
PALDGGQILF VLVGAVYRLI TRKTLDQKVL GYINMVGFVC LMGLMVVVAV SDVRKFIL
//
