ID A0A0G0IAX9_9BACT Unreviewed; 415 AA.
AC A0A0G0IAX9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:KKQ51667.1};
GN ORFNames=US72_C0013G0006 {ECO:0000313|EMBL:KKQ51667.1};
OS Microgenomates group bacterium GW2011_GWC1_38_12.
OC Bacteria.
OX NCBI_TaxID=1618512 {ECO:0000313|EMBL:KKQ51667.1, ECO:0000313|Proteomes:UP000034948};
RN [1] {ECO:0000313|EMBL:KKQ51667.1, ECO:0000313|Proteomes:UP000034948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:KKQ51667.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBUB01000013; KKQ51667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0IAX9; -.
DR Proteomes; UP000034948; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KKQ51667.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..186
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 394..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45364 MW; 35BE76549EF61C6E CRC64;
MPKINYIKFN LRLVRNVLAL AIIISISFGI GYLSGFKGFK AEVKFTDVKI AREVPEDKNV
NLDLFWKVWD TLGVKYYDKS KLIPSEMVYG AIRGMVSAVG DPYTVFLPPQ EKKVVQEDLQ
GTFEGVGIQI GFKGTRLAVI APLPGTPAEK SGVKAGDLIL VIRDESRRID QGTDGISITD
AVEAIRGPAG TTVTLTLLRD GKDEPFDVDI TRQSINVPSI VLEYKGDNNS IAYIKVLKFS
AETSGEWEEA VIELVKRNDL KGIIIDLRNN PGGYLEKAVE LASDFLENKD TVVVEEGAGG
VKNDYKVEKI GRLRKVNLVI LINEGSASAS EIMAGALRDH DRAKLVGSTT FGKGTIQEPM
DVDGGAGLHI TIAKWLTPSG FWVNEGGLKP DVEIEDKEDT EEDEQLQKAV ELLGP
//
