ID A0A0G0SZX7_9BACT Unreviewed; 404 AA.
AC A0A0G0SZX7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carboxy-terminal-processing protease {ECO:0000313|EMBL:KKR70314.1};
GN ORFNames=UU13_C0008G0010 {ECO:0000313|EMBL:KKR70314.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWB1_40_7.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618744 {ECO:0000313|EMBL:KKR70314.1, ECO:0000313|Proteomes:UP000034452};
RN [1] {ECO:0000313|EMBL:KKR70314.1, ECO:0000313|Proteomes:UP000034452}
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:KKR70314.1}.
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DR EMBL; LBZL01000008; KKR70314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0SZX7; -.
DR PATRIC; fig|1618744.3.peg.357; -.
DR Proteomes; UP000034452; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KKR70314.1};
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 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..172
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 404 AA; 44433 MW; A19D882F03F63854 CRC64;
MENLSKTRYF TIAILFATLS FVFGVYFGDR NRPEIDKILG ISGKELQVAT TADFSPFWKV
WNTMSKKYPL ADEISDQDRV YGAISGLVGS LNDPYSVFFT PDEAKSFEEE ITGNFDGIGM
EVGIKDKVLT VIAPLKDTPA YKADIKSGDK ILKINEKVTT GLSIEEAIKL IRGPKGTAVT
LTIFRDGIKQ PKEIKIVRDT IEIPTLDTEM RKDGIFVIKL YSFSANSVNL FRNAIKQFVD
SESDKLLLDL RGNPGGYLDA AVDMASWFLK GGTVIVTEDY GNNKAPEIFR SKGYDIFNNK
LKFVILIDGG SASASEILAG AMQDNGRAKL VGAQSFGKGS VQEVVDITSD TILKITVANW
LTPNGTSISE KGLTPDYPVE ITQKDIDAQK DPQMDKAIQL LINN
//
