ID A0A1F6DYB0_9BACT Unreviewed; 363 AA.
AC A0A1F6DYB0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=A3D71_02590 {ECO:0000313|EMBL:OGG66434.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_20.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798497 {ECO:0000313|EMBL:OGG66434.1, ECO:0000313|Proteomes:UP000177652};
RN [1] {ECO:0000313|EMBL:OGG66434.1, ECO:0000313|Proteomes:UP000177652}
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:OGG66434.1}.
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DR EMBL; MFLK01000007; OGG66434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DYB0; -.
DR STRING; 1798497.A3D71_02590; -.
DR Proteomes; UP000177652; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..178
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 363 AA; 38016 MW; C41E33FF394977C4 CRC64;
MVTALLVIAI LVLLIVAHEL GHFFAAKIFG VRVEEFGVGY PPRAFRFGKI GDTEYTLNWI
PFGGFVRLFG DAGETQHGRG SFVDAPRWKQ AIVLVAGVTA NVLVAYLLFA SALHLGVPKA
VDSANPGQDA RLIVADVVPG SPASIVGIKP GDEITGVSDE KGAIVGELTA QGVVDFVRAR
AGKPVDISYI HAGTKSTVTM TPANAVLPKA AGQPALGVAL VLIAMEQEPW SVALVDAFHQ
TLGAFRMIAR DLWTLLQGAI HGAPDLSSIV GPVGIVGYVG DASQNGLGAV LMFAALISIN
LAIINLIPIP ALDGGRLFVL AIEAVMRRDA PKLAIQALNA LGVALIVLLM IVVTYNDITR
LFA
//
