ID A0A077LW97_9MICO Unreviewed; 453 AA.
AC A0A077LW97;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:CCH78006.1};
GN ORFNames=BN12_2400020 {ECO:0000313|EMBL:CCH78006.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH78006.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH78006.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH78006.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH78006.1}.
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DR EMBL; CAJB01000158; CCH78006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077LW97; -.
DR STRING; 1194083.BN12_2400020; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000035721; Unassembled WGS sequence.
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:CCH78006.1};
KW Protease {ECO:0000313|EMBL:CCH78006.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035721}.
FT DOMAIN 349..436
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 45206 MW; 0F647F3A7A3B477F CRC64;
MNDLDENPKD ARRPADADGS PLWFGDSERS AQAFHPTSSM ATPTQEIPAG PSAPVFTQGQ
TEHAQPAKSR RPVELTAVAL LAALLASGGT YAATRVVGST DAQNPSTAQT SSDPGRGTSS
SAPVAQANAV APDWTATAAA VGPSVVAIAA MTSSGEDQGS GVILDRSGHI LTNNHVVSGA
QSVSVTLTDG RTYKASVRGT DATTDLAVVK LTTPPEGLKP ISIGDSSALK VGQPVMAVGN
PLGLAGTVTT GIVSALDRPV KTSSQEQADP TNPFGQPQTS EPVVTNAIQT SAAINPGNSG
GALVDASGKL IGINSAIATL SDGSTGQSGS IGIGFAIPIR EANAIAKQLI ATGTAQHAFL
GVSTSDGTAS DGSAQRDGAK ITSVVSGTPA AEAGIKAGDL VIAVDGVPVG SSDSLIANIR
ERTAGETVKI TVLRGGRTLN LKTKLVTKPS TSE
//
