ID A0A0Q2X9G9_MYCGO Unreviewed; 404 AA.
AC A0A0Q2X9G9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=AO501_10255 {ECO:0000313|EMBL:KQH77852.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH77852.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH77852.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH77852.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) 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:KQH77852.1}.
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DR EMBL; LKTM01000286; KQH77852.1; -; Genomic_DNA.
DR RefSeq; WP_055579261.1; NZ_LKTM01000286.1.
DR AlphaFoldDB; A0A0Q2X9G9; -.
DR STRING; 1778.A9W97_27570; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000051677; 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 ECO:0000313|EMBL:KQH77852.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KQH77852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051677};
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..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..203
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 404 AA; 42933 MW; BDB472D558D90DEE CRC64;
MMFVIGIVLF ALAILISVAL HECGHMWAAR ATGMKVRRYF VGFGPTLWST QRGETQYGFK
AIPAGGFCDI AGMTPVEELA PDEQDRAMYK QATWKRVAVL FAGPGMNFVI CLVLLYAIAL
VWGLPNLHPS NKAIVGETGC VAQEISQGKL DKCDGPGPAA LAGLRPGDVV VKVGDTPVST
FEDMATAVRK MHGSVPIVVD RDGKTITTNV TVESTRRYVP TGQGNQLEPA NVGAIGVGAP
RNEPTRYNVL SAAPATVVFA GQLTVEVGKS LAAIPTKVGA LFHAIGGGQR DPQTPMSVVG
ASIVGGDTVD HGLWVAFWFF LAQLNLVLGA INLLPLLPFD GGHIAVAVFE KIRNAIRTAR
GKVAAAPVNY LKLMPATYVV LIFVVGYMLL TVTADLVNPI RLFQ
//
