ID A0A0U2UFL9_9BACL Unreviewed; 519 AA.
AC A0A0U2UFL9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN ORFNames=IJ22_03160 {ECO:0000313|EMBL:ALS20705.1}, PN4B1_06380
GN {ECO:0000313|EMBL:GCL70736.1}, SAMN05421868_104204
GN {ECO:0000313|EMBL:SDI24750.1};
OS Paenibacillus naphthalenovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS20705.1, ECO:0000313|Proteomes:UP000061660};
RN [1] {ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS20705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS20705.1};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALS20705.1, ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS20705.1,
RC ECO:0000313|Proteomes:UP000061660};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
RN [4] {ECO:0000313|EMBL:SDI24750.1, ECO:0000313|Proteomes:UP000182184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR-N1 {ECO:0000313|EMBL:SDI24750.1,
RC ECO:0000313|Proteomes:UP000182184};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:GCL70736.1, ECO:0000313|Proteomes:UP000299945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B1 {ECO:0000313|EMBL:GCL70736.1,
RC ECO:0000313|Proteomes:UP000299945};
RA Ha-Thanh L.T., Ngoc-Thi T.V., Shintani M., Moriuchi R., Dohra H.,
RA Hoang-Loc N., Kimbara K.;
RT "Isolation and characterization of a moderate thermophilic Paenibacillus
RT naphthalenovorans strain 4B1 capable of degrading dibenzofuran from dioxin-
RT contaminated soil in Vietnam.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might be efficient in the degradation of transiently
CC denatured and unfolded proteins which accumulate in the periplasm
CC following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP013652; ALS20705.1; -; Genomic_DNA.
DR EMBL; BJCS01000002; GCL70736.1; -; Genomic_DNA.
DR EMBL; FNDY01000004; SDI24750.1; -; Genomic_DNA.
DR RefSeq; WP_062406750.1; NZ_FNDY01000004.1.
DR STRING; 162209.IJ22_03160; -.
DR KEGG; pnp:IJ22_03160; -.
DR PATRIC; fig|162209.4.peg.333; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000061660; Chromosome.
DR Proteomes; UP000182184; Unassembled WGS sequence.
DR Proteomes; UP000299945; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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; 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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 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, ECO:0000313|EMBL:SDI24750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061660};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..486
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 55598 MW; C2C7EF8588660A63 CRC64;
MDNNNKNGNP LYDFFGRAND GSSHHKEQEI DDKQEMKEEK AADIERHSSH YFSYGPFKPG
ESAAARENAG SPPVEVTPPK PLRTYSFHSP EEPNITNGGM GNWQVGKPKR SGSFRTIFAS
FMAGVVVVGS LMFASDKMNL FTGAEGVMNS GGSNGSIPAA SSNNGGVQPS ALDISRPNSV
SSIVQQASPA VVKIETKVKP KASSRTGNPF FDDPFFRQFF GDNGGQQPDS DQLQPGGMGT
GFIFEKSGYI LTNEHVIDGA DEIWVYVQGY EKPFKAELLG NSYDLDLAAL KIKGDKDFPT
LPLGNADNLN VGDWVVAIGN PYGFDHTVTV GVLSAKERPI SIPDTNGTRE YKHLLQTDAS
INPGNSGGPL LNLNGEVVGI NTAVSSQAQG IGFAIPTSTI NAVLDNLKNN VEIPKEPAPY
IGVRLGDVQK DWVADLKLPN TDGAIVSDVE RRSPAFTAGI RPYDVIVEVN GAKVKTSAEA
VSAIQKLKVG DKATIGVMRD GQKINIEVTI GDRNAQKQQ
//