ID A0A3P1SE11_9ACTO Unreviewed; 412 AA.
AC A0A3P1SE11;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=RIP metalloprotease {ECO:0000313|EMBL:RRC95140.1};
GN ORFNames=EII11_06995 {ECO:0000313|EMBL:RRC95140.1};
OS Schaalia canis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=100469 {ECO:0000313|EMBL:RRC95140.1, ECO:0000313|Proteomes:UP000280444};
RN [1] {ECO:0000313|EMBL:RRC95140.1, ECO:0000313|Proteomes:UP000280444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH770 {ECO:0000313|EMBL:RRC95140.1,
RC ECO:0000313|Proteomes:UP000280444};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRC95140.1}.
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DR EMBL; RQZF01000006; RRC95140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1SE11; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000280444; 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 SMART; SM00228; PDZ; 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:RRC95140.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RRC95140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280444};
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 122..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..219
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 412 AA; 43074 MW; 4561219D1C689DF5 CRC64;
MSYVIGILVI VVGLLISVAI HELGHMLPAK RFGVPVPVFS VGFGPLLWEK EWRGTRYGLR
AIPLGGYVRI VGMYAPARPG TPLLNKKGEL TLAEEARRES AAEIPEGMED RAFYRLSAPK
KFAVMFGGPV TNLILSAVLF AVVLMGIGVP AASPTLAAVP ATVTAVSGEV PGPAAAAGIE
AGDRITAVGE TPVERWSDLT SALNNSAGEP LSVTIDRNGE PQTVTVTPVK LEDGRWVIGV
GAGVEYVSAT PRRVLEVTWA TFTGTASVVT RLPVAVWEVL TSLVTGSERD PAGVMSVVGV
SRIAGEVASG EGVFATTDYR ATVATLLSLL ASLNMALFVF NLLPVPPLDG GHIVGAIFEG
VRRTVARLRG RPDPGPADTA RLVVVTYVMG ALLIGMSVIL MVADIVKPVT IG
//
