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Database: UniProt
Entry: A0A2I2L256_9ACTN
LinkDB: A0A2I2L256_9ACTN
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ID   A0A2I2L256_9ACTN        Unreviewed;       399 AA.
AC   A0A2I2L256;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Zinc metalloprotease Rip1 {ECO:0000313|EMBL:SNQ51985.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:SNQ51985.1};
GN   Name=rip {ECO:0000313|EMBL:SNQ51985.1};
GN   ORFNames=FRACA_890013 {ECO:0000313|EMBL:SNQ51985.1};
OS   Frankia canadensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ51985.1, ECO:0000313|Proteomes:UP000234331};
RN   [1] {ECO:0000313|EMBL:SNQ51985.1, ECO:0000313|Proteomes:UP000234331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ51985.1};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZMO01000557; SNQ51985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2L256; -.
DR   Proteomes; UP000234331; 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, ECO:0000313|EMBL:SNQ51985.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:SNQ51985.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SNQ51985.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234331};
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        101..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..199
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   399 AA;  42455 MW;  5AAFB4D6973A82E5 CRC64;
     MEAGLMEILG IVAFAAALLV SVVAHEGGHF VTARHYGMKA SKFFVGFGPT IWSRQRGETE
     YGVKLIPAGG FVKIEGMTPL EEIDPADEPR AFHNARARAR LVVMSAGSVV HFIIAIVLIY
     GVLVTLGTTR VSETKIGATS CVATTASCSG PGPAAAAGLR PGDRIVSFDG VAVSTWQDFT
     RRVRGHGAGP ATLVVERDGR DLTLRPDLVE VLRDRETGQA GNDRVGALGV KPGLDTERYG
     PLEAVPRTFD VIGSGFTGMY DTLTHRIDDL GKIFSKDRDP EGFISVVGAA RIGGDVVSAP
     DTSGTDRVRQ FLILVAAINL AVGIFNLLPL LPLDGGHIAV LGFEQARHGL RRLRGYRGPV
     KKVDFAKLLP ATYATVVVLL GFSLLLLSAD IVNPIRLNQ
//
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