ID A0A1G2K4Y5_9BACT Unreviewed; 356 AA.
AC A0A1G2K4Y5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|SMART:SM00228};
GN ORFNames=A2131_02335 {ECO:0000313|EMBL:OGZ93518.1};
OS Candidatus Sungbacteria bacterium GWC2_49_10.
OC Bacteria; Candidatus Sungbacteria.
OX NCBI_TaxID=1802263 {ECO:0000313|EMBL:OGZ93518.1, ECO:0000313|Proteomes:UP000177392};
RN [1] {ECO:0000313|EMBL:OGZ93518.1, ECO:0000313|Proteomes:UP000177392}
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:OGZ93518.1}.
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DR EMBL; MHQB01000035; OGZ93518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2K4Y5; -.
DR Proteomes; UP000177392; 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..191
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 356 AA; 38887 MW; A7E155E4AF06F874 CRC64;
MTLLFILFVI FLISILILVH EWGHFFSARM LKVKVEEFGF GFPPRVFSKV RNGVRYSFNL
LPFGGFVKIF GEHGEGEAAP ESFAGRPVWQ RFIILAAGVL MNLVLAWVLF SVASGIGMPE
IVDGEGSAIP VSVLSVAPGS PAESVGVKFG DAILRISQSG DSIAVSSEED VVSFIDAHKG
EEVTLSLRRG EEIKDISVLA RENPPDGQGS VGISMGRLDV VSVPWYLAPV EGAKTLGRSI
MLTIYGFWYL LSELVRGNTS IPVSGPVGIF VFANDIRPLG VSFFLHFMGI LSVNLAILNF
LPIPALDGGR VFFLLIEKLR GRRISAESEN IAHTIGFVVL IFLMVLVTYR DVTMFF
//
