ID A0A1G8YUC2_9MICO Unreviewed; 442 AA.
AC A0A1G8YUC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:SDK05590.1};
GN ORFNames=SAMN05216282_102270 {ECO:0000313|EMBL:SDK05590.1};
OS Cryobacterium psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK05590.1, ECO:0000313|Proteomes:UP000198701};
RN [1] {ECO:0000313|EMBL:SDK05590.1, ECO:0000313|Proteomes:UP000198701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK05590.1,
RC ECO:0000313|Proteomes:UP000198701};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFU01000002; SDK05590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8YUC2; -.
DR STRING; 386301.SAMN05216282_102270; -.
DR Proteomes; UP000198701; 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.
DR PROSITE; PS50106; PDZ; 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:SDK05590.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDK05590.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198701};
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 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..221
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 442 AA; 46195 MW; 32FB75F35066113E CRC64;
METVLLFILG VVVVIVGLAL SIGLHEIGHL VPAKAFGVKV TQYMVGFGPT LWSRRKGETE
YGVKAIPLGG YISMIGMFPP VKGGAARTSG TGFFNTLVQD ARSSSADSIG EGEEARAFYR
LPVFKRVIIM LGGPTMNLLI GIILFSIVLM GFGTAQASTT VGSVSECVLP ATSVRQTCDA
SDEPAPGAAA GLQPGDRIVS VNGTPIATWE QSTAIIRESP GTPLEFVVER DGEDVALTIT
PKLTERYVMD EAGQIEEDAS GQPVTTEVGF VGIGPASELV QQPATAVLPA VGDNIVRVGQ
MILNLPQRLV EVANAAFGPG ERDPNGPISV VGVGRVAGEI TSIDSVPVAS KVASLLGLLG
SVNIALFVFN LIPLLPLDGG HVAGALWEGI RRFFAKLFKR PVPGPVDTAK LMPLTFAVVI
VLGAMSLLLI YADIVKPISI FG
//
