RIP1_MYCBP
ID RIP1_MYCBP Reviewed; 404 AA.
AC A1KML4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Zinc metalloprotease Rip1;
DE EC=3.4.24.-;
DE AltName: Full=Regulator of sigma KLM proteases;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2-type intramembrane protease;
DE AltName: Full=site-2 protease Rip1;
DE Short=S2P protease Rip1;
GN Name=rip1; OrderedLocusNames=BCG_2891c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-21 AND ASP-340.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=16034419; DOI=10.1038/nature03713;
RA Makinoshima H., Glickman M.S.;
RT "Regulation of Mycobacterium tuberculosis cell envelope composition and
RT virulence by intramembrane proteolysis.";
RL Nature 436:406-409(2005).
CC -!- FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves
CC type-2 transmembrane proteins within their membrane-spanning domains.
CC Cleaves PbpB (PBP3, FtsI); cleavage is inhibited by Wag31-PbpB
CC interaction. Probably also cleaves anti-sigma factors RskA, RslA and
CC RsmA. {ECO:0000250}.
CC -!- FUNCTION: 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 (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in
CC M.tuberculosis) is first cut extracytoplasmically (site-1 protease,
CC S1P), then within the membrane itself (site-2 protease, S2P, this
CC entry), while cytoplasmic proteases finish degrading the regulatory
CC protein, liberating the effector protein (ECF sigma factors SigK, SigL
CC and SigM) (Probable). {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Cells have altered colony
CC morphology, lacking cording associated with virulence.
CC {ECO:0000269|PubMed:16034419}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AM408590; CAL72880.1; -; Genomic_DNA.
DR RefSeq; WP_011799297.1; NC_008769.1.
DR AlphaFoldDB; A1KML4; -.
DR MEROPS; M50.005; -.
DR KEGG; mbb:BCG_2891c; -.
DR HOGENOM; CLU_025778_1_2_11; -.
DR OMA; GPTQYNP; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..404
FT /note="Zinc metalloprotease Rip1"
FT /id="PRO_0000422673"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
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:0000250"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 21
FT /note="H->A: Does not restore cording to deletion mutants."
FT /evidence="ECO:0000269|PubMed:16034419"
FT MUTAGEN 340
FT /note="D->A: Does not restore cording to deletion mutants."
FT /evidence="ECO:0000269|PubMed:16034419"
SQ SEQUENCE 404 AA; 42912 MW; 6099C3B8DD053E84 CRC64;
MMFVTGIVLF ALAILISVAL HECGHMWVAR RTGMKVRRYF VGFGPTLWST RRGETEYGVK
AVPLGGFCDI AGMTPVEELD PDERDRAMYK QATWKRVAVL FAGPGMNLAI CLVLIYAIAL
VWGLPNLHPP TRAVIGETGC VAQEVSQGKL EQCTGPGPAA LAGIRSGDVV VKVGDTPVSS
FDEMAAAVRK SHGSVPIVVE RDGTAIVTYV DIESTQRWIP NGQGGELQPA TVGAIGVGAA
RVGPVRYGVF SAMPATFAFT GDLTVEVGKA LAALPTKVGA LVRAIGGGQR DPQTPISVVG
ASIIGGDTVD HGLWVAFWFF LAQLNLILAT INLLPLLPFD GGHIAVAVFE RIRNMVRSAR
GKVAAAPVNY LKLLPATYVV LVLVVGYMLL TVTADLVNPI RLFQ
