ID W7J1W4_9PSEU Unreviewed; 393 AA.
AC W7J1W4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Heat shock protein HtrA {ECO:0000313|EMBL:EWC60084.1};
GN ORFNames=UO65_4650 {ECO:0000313|EMBL:EWC60084.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC60084.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC60084.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC60084.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EWC60084.1}.
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DR EMBL; AYXG01000173; EWC60084.1; -; Genomic_DNA.
DR AlphaFoldDB; W7J1W4; -.
DR STRING; 909613.UO65_4650; -.
DR PATRIC; fig|909613.9.peg.4652; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
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; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Stress response {ECO:0000313|EMBL:EWC60084.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 299..389
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 39013 MW; D46D8EE6791F0D0E CRC64;
MLYGSAAQHP GYPAAPYQQQ HQTGQLQTAP PEQRRRAGGL VAGMTVLALL VGGGAGAAGG
YLVAQDNDTG SPAATALNTP PTAQQTGSAP AGSVEAVAAK VLPSVVQLQV RGPSSAGEGS
GFVISGDGLI VTNNHVVEVA ASGGQIEAVF QDGRTAKATI VGRDPTSDLA VVRAQGVTDL
PVAELGRSDD LRVGQPVVAI GSPFELAGTV TSGIVSSLQR PTRAGGENGS QATVMDAIQT
DAAINPGNSG GPLVNMAGQI IGINSAIYSP SSSASAQGGS VGIGFAIPIN QARRTADEIV
KTGKATQTVL GVSVRDNADG GALVADVVAG GPGEKAGLKQ GDVVTQLDDR RIDSADALVA
AVRSHAPNDT VKLVVGANNT VPVTLGGQPV ELK
//
