ID W2EJV0_9ACTN Unreviewed; 435 AA.
AC W2EJV0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=MPTA5024_36290 {ECO:0000313|EMBL:ETK31221.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK31221.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK31221.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK31221.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(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:ETK31221.1}.
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DR EMBL; AWEV01000290; ETK31221.1; -; Genomic_DNA.
DR RefSeq; WP_051459059.1; NZ_KI866527.1.
DR AlphaFoldDB; W2EJV0; -.
DR STRING; 316330.MPTA5024_36290; -.
DR PATRIC; fig|316330.3.peg.6985; -.
DR HOGENOM; CLU_020120_3_7_11; -.
DR OrthoDB; 73775at2; -.
DR Proteomes; UP000018869; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..388
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 43364 MW; A577265665466D75 CRC64;
MTDHTRSHDA SDRPEPSPGG EEPRWGPLGG TPEPPPPPPP LPGAYGMGPE WAPPPAPAEP
PQRGLNLALF AALAVVIALV AGGVASWGTF LLTRSPSGTD PGYSLATPSA APTGRAPDSV
AGVAAKVLPS VVSLEVRGSG EAGTGSGFVI KGGYVVTNNH VVAVAAQGGE IRIRFADRSS
LGARIVGRDP NSDIAVVKPD GPIRAPELPL GNSDGVVVGD PVIAIGSPLG LMGTVTTGIV
SSLNRPVEAG GSTGSDYALI NAIQTDAAIN PGNSGGPLVN AAGEVIGVNS AIATLGGSAG
FGQQTGSIGL GFAIPVNQVR RIAQELITSG TARTSRIGIS IDQSYQGQGV RIATQATGGA
TPVTPGGPAD QAGLRPGDVI LEVDGRPVGD SRELIVSIRS RAPGDRVEIK FQHDGEVRTA
TVTVGAAPVP SAGPS
//
