ID A0A1Y4NE15_9FIRM Unreviewed; 357 AA.
AC A0A1Y4NE15;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:OUP79076.1};
GN ORFNames=B5F09_00425 {ECO:0000313|EMBL:OUP79076.1};
OS Erysipelatoclostridium sp. An173.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP79076.1, ECO:0000313|Proteomes:UP000196550};
RN [1] {ECO:0000313|Proteomes:UP000196550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
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:OUP79076.1}.
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DR EMBL; NFKR01000001; OUP79076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NE15; -.
DR Proteomes; UP000196550; 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; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
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; PF13180; PDZ_2; 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:OUP79076.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OUP79076.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196550};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..343
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 125..202
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 357 AA; 39003 MW; 9750632CF9D9AB51 CRC64;
MQTLINIIVF ILILGIVVLI HEFGHFITAK SFGVYCSEFS IGMGPKLFSK KIGETEYEIR
ALPIGGFVSM AGEADNEIEE FKDVPFERTI NGISCWKKVV VFLAGVFMNF ILSIVILIGV
YSFIEVQDNT PVIGSVSDNG PAMMAGIEAG DRITKIAYDG EEYIIGSYDD IREVMGKIES
DDKTVTVEVE LVRDSKTLTK QVNAQYSEES GMFILGVISG TRQLSFFEAV NYAFDQFKTL
SLLIFTTLGQ LFTDTANTIG QLSGPAGIYS TTAQITATGS ISQLLIFLAL ISTNVGIFNL
LPIPGLDGCQ VIFALVEKMI GRELPLKLRY ALQLAGLALV FALLIYVTIN DVSRILG
//
