ID G2NLF1_STREK Unreviewed; 498 AA.
AC G2NLF1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:AEN11260.1};
GN ORFNames=SACTE_3395 {ECO:0000313|EMBL:AEN11260.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11260.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN11260.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN11260.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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DR EMBL; CP002993; AEN11260.1; -; Genomic_DNA.
DR RefSeq; WP_014047240.1; NC_015953.1.
DR AlphaFoldDB; G2NLF1; -.
DR STRING; 862751.SACTE_3395; -.
DR MEROPS; S01.494; -.
DR KEGG; ssx:SACTE_3395; -.
DR PATRIC; fig|862751.12.peg.3532; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_7_11; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000001397; 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 132..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 402..482
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 48540 MW; 1ECBBDD370CBBB57 CRC64;
MSTDNEGNEN DAVPPAPSVP SVPPVPAAAP EGAPPVGDMP ASGTARPADA PTAQGPAAHQ
GDGTVPSASP YAQPQQPAQP PAPAQPPAGS AGWPPPPPAV PSYADGGSPQ PWGAPAHHAE
HGAPRKRRAG GLVAAVAVAA LVAGGIGGAL GYWAADSNAS GSSGSTTVAA SNSPKDFKRA
DGTVAGVAAK ALPSVVTIDA QSGEGEGGTG TGFVYDKEGH ILTNNHVVAS AADSGQLTAT
FSDGKKYGAE VVGRAEGYDV AVLKLKNAPD GLTPLALGDS DKVAVGDSTI AIGAPFGLSN
TVTTGIISAK NRPVASGDGS SSANSYMSAL QTDASINPGN SGGPLLDAGG AVIGINSAIQ
STSGGGVGQS QAGSIGLGFA IPVNQAKNVA EQLIKTGQPV YPVIGATVTM EEKSGGAVIS
DDGAGGTPAV TPNGPAAKAG LKAGDVITKF NDTVVESGPT LIGEIWTHKP GDKVTLTYQR
GGKTSTVDVV LGERKGDS
//
