ID A0A095ZG12_9CORY Unreviewed; 410 AA.
AC A0A095ZG12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=HMPREF1650_03415 {ECO:0000313|EMBL:KGF17612.1};
OS Corynebacterium freneyi DNF00450.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1287475 {ECO:0000313|EMBL:KGF17612.1, ECO:0000313|Proteomes:UP000029548};
RN [1] {ECO:0000313|EMBL:KGF17612.1, ECO:0000313|Proteomes:UP000029548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00450 {ECO:0000313|EMBL:KGF17612.1,
RC ECO:0000313|Proteomes:UP000029548};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF17612.1}.
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DR EMBL; JRNE01000037; KGF17612.1; -; Genomic_DNA.
DR RefSeq; WP_035120836.1; NZ_JRNE01000037.1.
DR AlphaFoldDB; A0A095ZG12; -.
DR eggNOG; COG0750; Bacteria.
DR Proteomes; UP000029548; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029548};
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 104..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..212
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 410 AA; 43674 MW; 8BF5819294324825 CRC64;
MSFLLGVVLF ALGIAVTIAL HEWGHMRAAR ACGMRVRRYF IGFGPTVWST SRRHDGAGGH
VTEYGVKAVP LGGFCDIAGM TAQDPVAPEE EEHAMWRRPW WQRIAVLSGG VAMNLVVGVI
LIYVVAVAWG LPNLNADYSP RVQATQCVPA TQHADGTLSE CSGTGPAGDA GLRAGDVITS
VNGREVETYP QVIEAVGSSE SGPIEFTVER AGVTETITVQ PDVVERRTAD GTVVETPAVG
VLFQRPDNTL NEYTPLTAVP GALAFTVDMF GAVWDGLLSI PSKVPGVVAS IFGGERDQES
PMSVVGASRV GGEMVENDMW SGFLMMLANL NFFLALFNLV PLPPLDGGHI AVVVYEKLRD
LLRRLAGKPA LGPADYTKLM PVTMAFTAVL LTFGVIVIAA DVVNPIRLFG
//
