ID A0A132MNG7_9ACTN Unreviewed; 426 AA.
AC A0A132MNG7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=LI90_909 {ECO:0000313|EMBL:KWW99275.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99275.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) 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:KWW99275.1}.
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DR EMBL; LAXD01000001; KWW99275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132MNG7; -.
DR STRING; 1469144.LI90_909; -.
DR PATRIC; fig|1469144.10.peg.1026; -.
DR Proteomes; UP000070188; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..406
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 42884 MW; 2A7D562253AE672E CRC64;
MPASPVPGGA AAPASHGASG AAGGWGEPSG GPEYPWAPPA EEREVPGRRA RERARRGLGS
LIAVGLVAGL VGGGVGWFAS SQTNERIGGS YVELPTAQKG TTDRPPGTVA SIAEAVLPAV
VSISVSTESE EDTGSGFVIR PDGYILTNHH VVASALDGGT IEVRFPDART ATAKIVGQPD
AQSDLAVIKV DGMSGLVAAR LGNSDSVVVG DPVVAIGSPL GLAGTVTSGI ISAKDRPVTA
GGGREGESSF INALQTDAAI NPGNSGGPLV NGRGEVIGVN SAIATLGGGP FGGGQQGNIG
LGFAIPINQA KNIAEQIINK GRAVHPVLGV SLDPTYQGVG ARIIDDSQAR GGQRPVLPGS
PAEKAGLQPG DVIVQVDDRR ITTSTELVVT IRDKAPGSTV KITYKRGSET RTVDVTLATD
AQLNQR
//
