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Database: UniProt
Entry: A0A1Q8CU64_9PSEU
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ID   A0A1Q8CU64_9PSEU        Unreviewed;       304 AA.
AC   A0A1Q8CU64;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=BU204_08820 {ECO:0000313|EMBL:OLF17902.1};
OS   Actinophytocola xanthii.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF17902.1, ECO:0000313|Proteomes:UP000185596};
RN   [1] {ECO:0000313|EMBL:OLF17902.1, ECO:0000313|Proteomes:UP000185596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-183 {ECO:0000313|EMBL:OLF17902.1,
RC   ECO:0000313|Proteomes:UP000185596};
RA   Wang W., Yuan L.;
RT   "The draft genome sequence of Actinophytocola sp. 11-183.";
RL   Submitted (DEC-2016) 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   -!- 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:OLF17902.1}.
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DR   EMBL; MSIE01000013; OLF17902.1; -; Genomic_DNA.
DR   RefSeq; WP_075125097.1; NZ_MSIE01000013.1.
DR   AlphaFoldDB; A0A1Q8CU64; -.
DR   STRING; 1912961.BU204_08820; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000185596; 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   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185596};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  30489 MW;  AD2170C7FE7B8539 CRC64;
     MTETYLPPRQ PPVPPWTGTT QNYLPPLPPQ PPKRNRLRHR TVALLAAATL AAGGIGGTVG
     ALIGDDGATA TTTTATPTTA TTDTATEPTD VSDVVARVAA SVVQVNVTLA GGEGLGSGVI
     VGSDGRILTN NHVVAGAERI TVTLADGRTV DATVEGTDPS SDLAVIQAQG VSGLTAATFA
     DSDAVEVGDE VIAIGSPGGL QGTVTTGIVS ALDREVTVSG EEQRQSPLQP QRQAADTVTY
     HAIQTDASIN QGNSGGPLFD AEGRVIGINS AIYSPVSGPD GSAGSVGIGF AIPANTAQQL
     LSQL
//
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