ID D9TCT1_MICAI Unreviewed; 504 AA.
AC D9TCT1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADL48718.1};
GN OrderedLocusNames=Micau_5212 {ECO:0000313|EMBL:ADL48718.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL48718.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL48718.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002162; ADL48718.1; -; Genomic_DNA.
DR RefSeq; WP_013288330.1; NC_014391.1.
DR AlphaFoldDB; D9TCT1; -.
DR STRING; 644283.Micau_5212; -.
DR MEROPS; S01.494; -.
DR KEGG; mau:Micau_5212; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_4_11; -.
DR OrthoDB; 9788136at2; -.
DR Proteomes; UP000001908; Chromosome.
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; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 164..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..466
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 50361 MW; 256D84073B1F1315 CRC64;
MTDHETDPQR SPAPADAEPS HHTAELPRLE SGTSDSSSTP AAASVPADSP AAGTSTPAGH
TNPAESAGNT APAGPYPPQP ATPSAPPYPA SGQPHPWYGQ QHQQGGWNQQ TAAGYPSTQH
GGPVPSYQAQ PYQTQQGYQS YQPGQPMPQW GPQQPARPSR AGKFVGAGAL ALVLMLGSGA
AGGALALALD GDGPTRTYSA APVINSADLP KIAASVQDSI VTIMTNSGEG SGVILSADGF
VLTNNHVVAG AGGDTVRVVF ADGKSASAKI VGTDPKTDLA VVQASGVSNL KAAKFGDSDA
MQVGDQVLAL GSPLGLQGSV TAGILSARDR TIQAGEGGQQ NPQQGASSIS GLLQTDAPIN
PGNSGGALVN TRGEVIGINT AIATAGQGST GNIGVGFAIP SNKAKNVAEK LQRGEKISHP
SLGVSVNGAE DGGALVAAVT PGSPAEKAGI QRGDVITKFG DKVINDSNDL VGAVQAGKVG
DRVEVQYKRN GSTENATVTL AETS
//
