ID A0A1J4VJZ9_9BACT Unreviewed; 481 AA.
AC A0A1J4VJZ9;
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=AUJ70_01130 {ECO:0000313|EMBL:OIO34423.1};
OS Candidatus Omnitrophica bacterium CG1_02_40_15.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805284 {ECO:0000313|EMBL:OIO34423.1, ECO:0000313|Proteomes:UP000183570};
RN [1] {ECO:0000313|EMBL:OIO34423.1, ECO:0000313|Proteomes:UP000183570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_40_15 {ECO:0000313|EMBL:OIO34423.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO34423.1}.
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DR EMBL; MNVP01000021; OIO34423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VJZ9; -.
DR STRING; 1805284.AUJ70_01130; -.
DR Proteomes; UP000183570; Unassembled WGS sequence.
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 281..360
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 385..453
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 481 AA; 52453 MW; B5D86AEFC394AB6F CRC64;
MRKSVIFILT AFLSISLVYD LYAEPPKEAL SLQDAFVKVS KDVGQAVVSI STEHTERYQT
RYYPFAQFED QFSNDFFNDF FVEGPQREFK RIGLGSGFII NKEGYIITNE HVIHGADKIT
VTLPDAREFE ASLTGSDAYS DMAVIKIEPK GELSFAKLGN SDDIQIGNWA IAIGNPFAFA
VKNPEPTITV GVISALHRSL PMTDKRTREY SDLIQTDAAI NPGNSGGPLV NIYGEVIGIN
VAIFTLSGGS EGIGFAIPIN AAKKIINDLM QGKKVLYGWL GVIIQDMDVN LASYFGLSDK
TGVLVSKIVE TSPAEKAGLR PGDIIISLDN DIIKNTESLI IALLKKSVGD KVTLGVTRDS
KLYSVIVEIG KRPEDAAMVA QKKTEPQVTK KSAKSWRGLE VTDITAEIAQ HFKISAESGV
IVLSIEPGSP SERSGIRPGD VIYEINRTSV KNIKDYSLVV DKVSGDALIG TYRGYVVLKE
K
//