ID A0A1F6D8K6_9BACT Unreviewed; 421 AA.
AC A0A1F6D8K6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=A2765_05120 {ECO:0000313|EMBL:OGG57784.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_56_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798487 {ECO:0000313|EMBL:OGG57784.1, ECO:0000313|Proteomes:UP000176377};
RN [1] {ECO:0000313|EMBL:OGG57784.1, ECO:0000313|Proteomes:UP000176377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG57784.1}.
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DR EMBL; MFLA01000045; OGG57784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6D8K6; -.
DR Proteomes; UP000176377; 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};
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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..204
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 421 AA; 45199 MW; 9CBF2878C34DAC4A CRC64;
MQEEKYGLSA LAIGAILLLA VGFAGGLILG NSGSLRSMLP AAVAQSLGID GPPQGVDLSP
VWKAWQIMDE KFVPASVPTT TASTSAPVIA GTPQEKRVYG MISGMAESLG DPYTFFLPPV
EQKQFEEDLS GNFEGVGMEI AVRDEVLTVV APLKGTPAER AGIKPDDRVL EIDDNDTHNM
DVTTAVNLIR GTKGTEVRLL ISREGWAEPK EIKVMRDVIN VPIVESEKRA DGTYVISLHT
FTSNSPQLFR DALRQFVNSG SNKLILDLRG NPGGYLEASV DMASWFLPTG KIVVTEDYAG
HADNIDHRSR GYDIFNDNLK AVILVDKGSA SASEILAGAL RHYGVAKLVG ATTFGKGSVQ
ELIPITENTG LKITVARWLL PDGTQIPKTG ITPDVEVKIS EEDVKAGKDP QMDKAVEMLG
K
//
