ID RIP1_MYCLE Reviewed; 404 AA.
AC Q9CBU4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Zinc metalloprotease Rip1;
DE EC=3.4.24.-;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2 protease Rip1;
DE Short=S2P protease Rip1;
DE AltName: Full=Site-2-type intramembrane protease;
GN Name=rip1; OrderedLocusNames=ML1582;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves
CC type-2 transmembrane proteins within their membrane-spanning domains.
CC Regulated intramembrane proteolysis (RIP) occurs when an
CC extracytoplasmic signal (possibly oxidative stress) triggers a
CC concerted proteolytic cascade to transmit information and elicit
CC cellular responses. The membrane-spanning regulatory substrate protein
CC is first cut extracytoplasmically (site-1 protease, S1P), then within
CC the membrane itself (site-2 protease, S2P, this entry), while
CC cytoplasmic proteases finish degrading the regulatory protein,
CC liberating the effector protein. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AL583922; CAC30533.1; -; Genomic_DNA.
DR PIR; H87106; H87106.
DR RefSeq; NP_302093.1; NC_002677.1.
DR RefSeq; WP_010908414.1; NC_002677.1.
DR AlphaFoldDB; Q9CBU4; -.
DR STRING; 272631.gene:17575423; -.
DR MEROPS; M50.005; -.
DR KEGG; mle:ML1582; -.
DR PATRIC; fig|272631.5.peg.2983; -.
DR Leproma; ML1582; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_2_11; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..404
FT /note="Zinc metalloprotease Rip1"
FT /id="PRO_0000088448"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 121..203
FT /note="PDZ"
FT ACT_SITE 22
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 404 AA; 42875 MW; F14169D1B385110C CRC64;
MMFALGIVLF AIAILISVAL HECGHLWVAC ATGMKVRRYF VGFGPTLWST RRGETQYGIK
AVPLGGFCDI VGMTSVEKLE PDESDRAMYK QATWKRVAVL FAGPAMNFVI CLVLIYGIAL
VWGLPNLHMP TRAVIGETAC VASELDQGKL GNCTGPGPAA LAGLRAGDVV VKIGDTTVST
FDDMAAVVRK LHGTVPIVFE RDGTAITSYV DITPTQRYMS KGKGSQLEPA TVGAIGVGAH
HLLPTHYGVF SALPATAAFA GDLTVEVGKA LVTIPTKLGA LVHAIGGGQR DPQTPMSVVG
ASIIGGDTVD HGLWVAFWFF LAQLNLILGA INLVPLLPFD GGHIAIAVFE RIRNLIRSAR
GVVVAAPVNY LKLMPATYVV LVFVVGYVLL TVTADLVNPI RLFQ
//
