ID A0A1M6IMD8_9ACTN Unreviewed; 427 AA.
AC A0A1M6IMD8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:SHJ35651.1};
GN ORFNames=SAMN02745244_02327 {ECO:0000313|EMBL:SHJ35651.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ35651.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ35651.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ35651.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQZG01000042; SHJ35651.1; -; Genomic_DNA.
DR RefSeq; WP_073188450.1; NZ_FQZG01000042.1.
DR AlphaFoldDB; A0A1M6IMD8; -.
DR STRING; 1123357.SAMN02745244_02327; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000184512; 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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:SHJ35651.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SHJ35651.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184512};
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..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..380
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 177..225
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 427 AA; 46355 MW; 3F057F1EDEFD6082 CRC64;
MTILITVLLA VLFFALIMAS IALHEIGHLV PAKLFGVKVT QYFVGFGKTL WSRTKGGTEY
GFKAFPLGGY VRLVGMYPPA KHNARPGWLT RLADQARSYE YEEITSADDG HLMYQKKTWQ
KIVIMLGGPM MNVLLAFLIF LGINVFHGTY QSTLTVAQVS ECVVRTDRED QTCKADDPLT
PASEAGVQVG DRLVSFNGVI LTDWTQMGDL IRDNRDGDAT VVVEREGREL TLPTVNTVLN
HVPDRLDPTR YVEAGFFGVS PTTEVVHGGP VATLEQMWTM TQQSAVALAS FPVRIYNVAA
DLVTGQPRDA NSPMSIVGAS RVAGEIGTSD TLSAGDKVAT WMSLLGSVNL FVALLNLVPL
LPLDGGHIAG AIYEWVKRNL ARLFGRPDPG HVDTARGLPI TYLVGGFLLL GGVVLILADI
IAPIQLF
//