ID K1YHV7_9BACT Unreviewed; 510 AA.
AC K1YHV7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
DE Flags: Fragment;
GN ORFNames=ACD_75C01368G0003 {ECO:0000313|EMBL:EKD36797.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD36797.1};
RN [1] {ECO:0000313|EMBL:EKD36797.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:EKD36797.1}.
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DR EMBL; AMFJ01032037; EKD36797.1; -; Genomic_DNA.
DR AlphaFoldDB; K1YHV7; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 307..393
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 422..477
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD36797.1"
SQ SEQUENCE 510 AA; 54924 MW; A139440665D2B844 CRC64;
ISMIYFQMRG HMLEENMKTG KKGRKTFIMF LLAFMIGFFV VSVVEVLRSS FVISGPGPDV
QVAAAGSTGE ISRAPLSFAD LAEKLKPSVV NISTTKTVRS GRPRTPFGQG SPFDRPFGGD
EFFERFFGDI PQREFKQRSL GSGFIITSDG YIFTNNHVIE QADKIIVKLS DGKEYEAKAI
GKDAKTDIAL IKIKTADSLP VADTGDSDKL RVGDWVMAIG NPFGLEQTVT AGIVSAKGRV
IGAGPYDNFI QTDASINPGN SGGPLFNMEG KVIGINTAIV AQGQGIGFAI PINMAKTILP
DLKAKGKVTR GWLGVSVQDI TEDIAKNIKL KDRSGTLIND VFKGDPADKA GLKSGDVITE
INGKKIKDTH ELLIIIAAFR VGETVKIKIL RDGQEKSVSI TVAERKDQGE IAAARNGGEA
FGMTVQEITP EIAKHLGLSI KKGVIVVDVQ EGSTADEVGI QPQDIILQVN KVKVESIKDY
AREIGKASEK GGILLLIQRG KARFFVPLTK
//
