ID K6X5C2_9ACTN Unreviewed; 510 AA.
AC K6X5C2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase S1 family protein {ECO:0000313|EMBL:GAB99602.1};
GN ORFNames=GONAM_10_00730 {ECO:0000313|EMBL:GAB99602.1};
OS Gordonia namibiensis NBRC 108229.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1208314 {ECO:0000313|EMBL:GAB99602.1, ECO:0000313|Proteomes:UP000035058};
RN [1] {ECO:0000313|EMBL:GAB99602.1, ECO:0000313|Proteomes:UP000035058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108229 {ECO:0000313|EMBL:GAB99602.1,
RC ECO:0000313|Proteomes:UP000035058};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia namibiensis NBRC 108229.";
RL Submitted (AUG-2012) 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:GAB99602.1}.
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DR EMBL; BAHE01000010; GAB99602.1; -; Genomic_DNA.
DR AlphaFoldDB; K6X5C2; -.
DR Proteomes; UP000035058; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..498
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 52962 MW; E3F7F9A88EF782F4 CRC64;
MADGTGSQDE DTSTPGGDAQ FARREDPPNT QRLTPGRARH SPVSPSTAQV FGRPSGVRGS
FATTPNNHSA PQPHVADPDP VLAEAFGRPP GSDETLQRDP LASYGQTDEE PRANDPWRDP
ESPARLVDPA LQTASSAPAT DPGPKLGVRD VLLGNRISWS ALATLAIIAL LIALVGGLMG
RWTAEVAAPL TTDSVELSTD DSGNGSAPRS SIAEVARAVE KSVVAIDVRA SGAYSTGSGF
VIDKAGYILT NNHVIAMAAN DKAAKLEVIF FDRQRVAARI VGRDPKTDLA VLKVENVKNP
TVSVLGSSAD LQIGEEVVAF GSPLGLNRTV TSGIVSATNR AVALTPDAES DTDAVIDAIQ
TDASINPGNS GGPLVNADAK VVGINTAGRL GAGGGSIGLG FAIPIDEAKP IAEALIRDGK
VNHAQIGINA SSVRNERVLG AQVRNVVSGG PAERAGVREN DVITSFNGRP IESADELNVA
VRTAKIGEEI PFQYWRDGRT FDGKITPQSD
//
