ID A0A0G0B426_9BACT Unreviewed; 434 AA.
AC A0A0G0B426;
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=Protease Do {ECO:0000313|EMBL:KKP58426.1};
GN ORFNames=UR51_C0006G0062 {ECO:0000313|EMBL:KKP58426.1};
OS Candidatus Moranbacteria bacterium GW2011_GWF1_34_10.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618715 {ECO:0000313|EMBL:KKP58426.1, ECO:0000313|Proteomes:UP000034605};
RN [1] {ECO:0000313|EMBL:KKP58426.1, ECO:0000313|Proteomes:UP000034605}
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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KKP58426.1}.
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DR EMBL; LBPM01000006; KKP58426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0B426; -.
DR STRING; 1618715.UR51_C0006G0062; -.
DR Proteomes; UP000034605; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KKP58426.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..421
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47585 MW; FFA1DCC033569827 CRC64;
MDNTEKKEEI KNEPVKETSN SALKNKIEKP RYRLPFRIWM IIILGMFLSS VLGGFFGFVA
GGFSGAFTDN VKNRIESKLG LNKNEVVTER GSVLREESAV IDVVEKNSAS VVNIVITKDV
PIFRNNGFDF FFNPFGYRNE NSQDTERQRV GGGTGFFVSN DGMIVTNKHV VSDEAAEYTV
ITTDEKEYKA TILARHPSLD IAIIKIEGNN FPVLNLGDSD NLKVGQSVIA IGNSLGEFSN
SVSLGIVSGL KRDITAGSGY GESERLSNII QTDAAINPGN SGGPLLDIRG NVIGINVAVA
QGVENIGFAL SVNDIKKTIE QVKRSGRISV PFLGIRYVIL DEEIQKENNL PYNYGALISR
GEKMTDFAVI PGSPADKAGL IENDIILEIN GQKIDANNQI NDMVASMEVG EKITMKIWRK
GNEQQLEATL EERR
//
