ID X5EBC9_9CORY Unreviewed; 412 AA.
AC X5EBC9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Zinc metalloprotease Rip1 {ECO:0000256|ARBA:ARBA00019897};
DE AltName: Full=S2P endopeptidase {ECO:0000256|ARBA:ARBA00032214};
DE AltName: Full=Site-2-type intramembrane protease {ECO:0000256|ARBA:ARBA00033476};
GN ORFNames=CGLY_07455 {ECO:0000313|EMBL:AHW63936.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63936.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW63936.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63936.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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; CP006842; AHW63936.1; -; Genomic_DNA.
DR RefSeq; WP_038548117.1; NZ_CP006842.1.
DR AlphaFoldDB; X5EBC9; -.
DR STRING; 1404245.CGLY_07455; -.
DR KEGG; cgy:CGLY_07455; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_2_11; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000023703; Chromosome.
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; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
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; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHW63936.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:AHW63936.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AHW63936.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703};
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 97..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..367
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 43736 MW; 331B04F672F1D9BD CRC64;
MSFALGVVLF ALGIGVTIAL HEAGHMVAAR VCGMRVRRYF IGFGPTVWST TRGHTEYGLK
AIPLGGFCDI AGMTVNDPWT EEEEPHLMIN KPAWKRVFVM MAGIIVNIVL GVLIIFGVAV
SFGLPSTEDK PIPATATQLL CSPVKEGDGT ENDPGCTGEG PAEASGVQVG DTFLTVDGRT
VEGFSDVIDA VQAAGRTAGE DGVALGDTVT VPATVERGGT DVDLNLQVQV VERGGEATGA
IGVQVELPPT EMVDYNPVAA VGGTADFTWN LGKQTVDALV HLPERYWPVV QSIFGAERQM
DSPVSVVGAS HAGGQLVEHE QWMSFLLLLA NLNFFLAVFN LVPLPPLDGG HAIVVIYEKI
RDRLRRLRGL APGGPVDYVK LMPLTYVATA VLLVFGLTVI VADVVNPLQL FP
//
