ID A0A1F5G2D4_9BACT Unreviewed; 368 AA.
AC A0A1F5G2D4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=A2696_02165 {ECO:0000313|EMBL:OGD85977.1};
OS Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_01_FULL_41_13.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797745 {ECO:0000313|EMBL:OGD85977.1, ECO:0000313|Proteomes:UP000177069};
RN [1] {ECO:0000313|EMBL:OGD85977.1, ECO:0000313|Proteomes:UP000177069}
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:OGD85977.1}.
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DR EMBL; MFBA01000008; OGD85977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5G2D4; -.
DR Proteomes; UP000177069; 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; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 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 93..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 139..194
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 368 AA; 40156 MW; E9C760C5B8471627 CRC64;
MAIIIFIIIL SVLVLIHEFG HFIAAKRAGI GVEEFGFGLP PRAWGKKIGE TIYSINWLPF
GGFVKLIGED PTDRHKHDKN SFYVKSIWQR AQVVVAGVAM NFILAVAIFY LVVFALGFKI
NLPFLIDHKF KFVNQSKQVL VADVASDSPA KAAGINPGDS IVAVNGGKVA SIGDLQKSVR
SSDGKTLILT IENPINNKTR TVSATPTFNR DLDAYALGVG LGELVVLNYQ TLPQRFFAGF
IHSYNTIDYS VKIFGQLIGF AIRERDITPV SEGVSGPIGI ATLTSQAVQL GSLSVLQLVG
LLSLNLAVLN ILPIPALDGG RFFFIIVEAV TRRRVHATFE KWVHSIGFAL LIALILLITY
NDVLKLLK
//