ID A0A0G1NN88_9BACT Unreviewed; 419 AA.
AC A0A0G1NN88;
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:KKU22079.1};
GN ORFNames=UX33_C0016G0006 {ECO:0000313|EMBL:KKU22079.1};
OS Candidatus Azambacteria bacterium GW2011_GWC1_46_13.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618619 {ECO:0000313|EMBL:KKU22079.1, ECO:0000313|Proteomes:UP000034569};
RN [1] {ECO:0000313|EMBL:KKU22079.1, ECO:0000313|Proteomes:UP000034569}
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:KKU22079.1}.
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DR EMBL; LCLU01000016; KKU22079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NN88; -.
DR Proteomes; UP000034569; Unassembled WGS sequence.
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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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 Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KKU22079.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 117..199
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 419 AA; 45892 MW; EC1E925710E9A322 CRC64;
MFSPKKYILL AVLLVAIFGL GVVIGQLGIL PFKIIPVGIP GVRFQEEPPE TFQIINKESG
KPKEIDFSRF WDVWQKVGET YATRKHLDSQ KMVYGAIAGM VKSLGDPYTV FFEPQEAKRF
EDDSKGSFEG IGAEIGIKKG VLTVIAPLEE TPAKKAGLMA GDKILKIDDT ITADLTIEEA
VRLIRGTKGT EVVLTVSRDA WTETKEIKIA RDVIKVPILK LEFKGDLAYL RLYQFTENSS
EEFTKAAGTI LASPAKGIVL DLRNNPGGYL DKAVDIAGWF LAQGQVVAME DFGNGQKETF
YSAGPAKLAE YKTVILVNQG SASASEILAG ALKENRGLKL IGEKTYGKGS VQQLFDFNDG
SSLKVTVAKW LTPNGRSISD EGLEADVKVE LKAEDLEKNL DPQLDKAIEL LKEQITNNK
//
