ID A0A1F8TVB4_9CHLR Unreviewed; 440 AA.
AC A0A1F8TVB4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|SMART:SM00228};
GN ORFNames=A3K41_14010 {ECO:0000313|EMBL:OGO76100.1};
OS Chloroflexi bacterium RIFOXYD12_FULL_57_15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797675 {ECO:0000313|EMBL:OGO76100.1, ECO:0000313|Proteomes:UP000178494};
RN [1] {ECO:0000313|EMBL:OGO76100.1, ECO:0000313|Proteomes:UP000178494}
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:OGO76100.1}.
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DR EMBL; MGOQ01000509; OGO76100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8TVB4; -.
DR Proteomes; UP000178494; 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; cd05709; S2P-M50; 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; 2.
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 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..256
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 440 AA; 48037 MW; 3968834B10B31E1D CRC64;
MIFFLAFAGM ILVHEFGHFI VARWFGIEVE EFGFGLPPRI LRLWRPKGSL TVGRRQIVIP
RNFDLPFDPQ EGLDHGVDVT ARRVDGKLIL DSIRLAAAED GQYRPAQVDP VESAGGKVTF
DGILKQVLQG TEFTLNWLPI GGFVRPKGEN DPNVQGGLAA ANAWKRLGVL FAGPTMNLLT
GLLVFLFLVR VDGYHDMSRV QLAEIAPDSP AEAAGMKVGD VVRQAAGQPV TDFASLSGIV
NAHLDQPVEF VLQRGGETLT VTATPRSQPP EGQGAVGIRM SEFVMPVETW GDTFRYGAVS
VYDQARALVL LPAKLLRGSS SPDEGRFIGM KGIYDIFNLT VSTDVQSREP LASAQPQAPT
FSTLYLIAAL TISIGLINLF PFPALDGGRI IFAIPEIIFR RRVPHQFENA VHAAGMILLL
LLMLYINVMD FVNPLVIPTP
//
