ID A0A1X7K2J0_9MICO Unreviewed; 596 AA.
AC A0A1X7K2J0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Putative serine protease PepD {ECO:0000313|EMBL:SMG34513.1};
GN ORFNames=SAMN06296010_1947 {ECO:0000313|EMBL:SMG34513.1};
OS Agreia pratensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=150121 {ECO:0000313|EMBL:SMG34513.1, ECO:0000313|Proteomes:UP000193244};
RN [1] {ECO:0000313|EMBL:SMG34513.1, ECO:0000313|Proteomes:UP000193244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2510 {ECO:0000313|EMBL:SMG34513.1,
RC ECO:0000313|Proteomes:UP000193244};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FXAY01000003; SMG34513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7K2J0; -.
DR STRING; 150121.SAMN06296010_1947; -.
DR Proteomes; UP000193244; 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 InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF00089; Trypsin; 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:SMG34513.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SMG34513.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 188..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..582
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 58587 MW; CF76A0EFF84A91BC CRC64;
MSENTDNPIN PAAAEGVDRD DTTNTGSSPA ATEHAPAFPH YAPSASGATP SSTHTSEPAK
EQNAPQISGT QQAPEGMTPP AATAPPAAPL AGSAPHPGYG HTPAAPQPTQ PVAQAHPAQA
TAAHYPAPHN QTQPHQAQPN QTQPTQAYAA APGNYGNGAF GQPPQQPPVA GAATSGAHAP
KRRGATMVIA ALAIAALVGG ASGAGITAWT LSQNQQSSTS SASGPQTITV NNADDASLAT
AVAAKASPSV VTISVNDGQS GGTGSGVILS DDGYVLTNTH VVTLDGATGK PTIQVTTNDG
RLFAGTLVGT DPVADLAVIK LDKAKDLTPI TWGDSTKLNV GDSVVAIGAP LGLSGTVTTG
IVSALNRAIT VASSAAPKGD DTESTPPDDN GGPGDGTKQN PYDFWNFDIP GQGGSEAPKQ
APATSSISLA VIQTDAAINP GNSGGALLND KGELIGINVA IASAGSSSGS GQSGSIGVGF
SIPAALAQRI SQEIIKDGAG SHGLLGASVG DASSDQALAS VTAGALVKEV SSGGAAEKAG
IKAGDVITAF NGIPVAGATD LTAQVRSLAA DSDAKLTVYR DGKNQDIDVK LGELTQ
//
