ID A0A399G1N6_9ACTN Unreviewed; 579 AA.
AC A0A399G1N6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:RII01432.1};
DE SubName: Full=Trypsin-like peptidase domain-containing protein {ECO:0000313|EMBL:UOE19424.1};
GN ORFNames=NI17_022320 {ECO:0000313|EMBL:UOE19424.1}, NI17_17980
GN {ECO:0000313|EMBL:RII01432.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII01432.1};
RN [1] {ECO:0000313|EMBL:RII01432.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII01432.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE19424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE19424.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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; JRUV01000281; RII01432.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE19424.1; -; Genomic_DNA.
DR RefSeq; WP_068690344.1; NZ_LIZN01000005.1.
DR AlphaFoldDB; A0A399G1N6; -.
DR STRING; 483545.GCA_001660385_04295; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000265719; Chromosome.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RII01432.1};
KW Protease {ECO:0000313|EMBL:RII01432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265719}.
FT DOMAIN 461..560
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 57674 MW; 30B2A0991CF45439 CRC64;
MSAIDRGSGS SMEEPERPVG PQADADGREN VTDTGAGEAS GSTARSEVPP SSSDAAPAAD
PHPGQQRETP EVRRSEVPLR PARHQGPFAP GHTAHQPGPG QHAPGQPGPD QSASGPPPSG
QHPSGPFGSG QHASGPHSSG PHAPAPSSEW ARQPEWFERA TAHQVQGHQQ HTGGWATPSP
RGAFSSHGGG FPPPPHDAPA MPGAAPPETG QRRRGRVVLV AAATALLTSL VVGPAASVAT
AYLVDGETTN STSSTSAATG DVSRVADKAL PSVVSISTAE GGGSGFIISS DGLIVTNNHV
VSGTGEVTVA FNDGSQAEAT TVGTDPVSDL AVIQAEGVSG LTPATLGDSD QVAVGARVVA
IGAPLGLSGT VTSGVISALE RPVNTGVSGQ QPDSPFTLPP EGEQDEPQAT TSTVIDAIQT
DAPINPGNSG GPLMNMDGEV IGINTAIATT SGGGLTQSGS IGLGFAIPIN QAKPTIDELV
TTGEATYAAI EAAVTVAEDG SGAELVDVTR GGAADQAGLQ AGDVIVGVGN RAVTDPNVLI
AEIRSHRPGD TVTVTYERDG RTAEAQVTLS AQSSSDIGN
//