ID A0A2T0ZXF7_9ACTN Unreviewed; 626 AA.
AC A0A2T0ZXF7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=S1-C subfamily serine protease {ECO:0000313|EMBL:PRZ41042.1};
GN ORFNames=CLV47_11275 {ECO:0000313|EMBL:PRZ41042.1};
OS Antricoccus suffuscus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Antricoccaceae; Antricoccus.
OX NCBI_TaxID=1629062 {ECO:0000313|EMBL:PRZ41042.1, ECO:0000313|Proteomes:UP000237752};
RN [1] {ECO:0000313|EMBL:PRZ41042.1, ECO:0000313|Proteomes:UP000237752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100065 {ECO:0000313|EMBL:PRZ41042.1,
RC ECO:0000313|Proteomes:UP000237752};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PRZ41042.1}.
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DR EMBL; PVUE01000012; PRZ41042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0ZXF7; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000237752; 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: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; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 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:0000313|EMBL:PRZ41042.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:PRZ41042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237752};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 277..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 533..616
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 63788 MW; 1338F07031D0CD1C CRC64;
MSNDDQSQSD RAAEPVTPSD AADGSTDSGG ASPGHLGTPR AQGGAVNSDS RSSQTVSAQS
LPPLAQDSSS PPQSSQSSQP SQSQASQSQS YPATPGDPQP RWQSGPPRPS SPQPLPAPAP
PQSAPGPTID FGRPQGVAGS FVQRPPQRPR GHRQAPPPPA VAQAFGRPPS ASGSFAPGNR
PAPRPSAPVP PVPPAYRAAF GRPQDAADLQ RPPGEKPYGL QIRESPWWKP DAPRDPWRDP
RSAASLTAPT SESAEPVDEG ILDTDKKRRR RIRVRDLPIR LGVVLGICAL ILGLAGGATG
FFLAKKAAES PLTKAEPQYQ KAADAPPPSD IAGVADKVQP SVVSIDVIAG NTGATGSGVV
IEADGYILTN NHVVSMAATS DQAKISVHFV DGSISPGKIV GRDQKSDLAV IKVDKPGLVP
IEIGKSAKLH VGDEVVAFGS PLGLAGTVTS GIVSALNRPM HLSGEGSDSD AYILAVQTDA
AINHGNSGGA LVDANGSLIG INSAIASSDA QGGSIGLGFA IPVDYAIQVA DSIIKTGKVE
HGDLQLAAQS VTDGSQNGAL IVRVDAGGAA DKAGLKAKDV IVQAGDTKVT AVADLMAVAY
LHKPGDKLML KVISGGTAKD VEVTLG
//
