ID A0A1G6Y479_9BURK Unreviewed; 489 AA.
AC A0A1G6Y479;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:SDD85102.1};
GN ORFNames=SAMN05444679_114116 {ECO:0000313|EMBL:SDD85102.1};
OS Variovorax sp. CF079.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDD85102.1, ECO:0000313|Proteomes:UP000198763};
RN [1] {ECO:0000313|EMBL:SDD85102.1, ECO:0000313|Proteomes:UP000198763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF079 {ECO:0000313|EMBL:SDD85102.1,
RC ECO:0000313|Proteomes:UP000198763};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; FMZU01000014; SDD85102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6Y479; -.
DR STRING; 1882774.SAMN05444679_114116; -.
DR OrthoDB; 8520726at2; -.
DR Proteomes; UP000198763; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDD85102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198763};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039341663"
FT DOMAIN 283..374
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 390..479
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 386..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 489 AA; 50995 MW; 3FB8D650DB6A4882 CRC64;
MNVRLNSPRA LVLALSAAGV IGAVGAGAYT SANAVNTPAP AVAAPMVTMP DFSTITTRNG
PAVVNISVTG TMKTSMEGVA GIPGMDPDDP MFEFFRRFQG QMGPRGKQQQ QREMPVRGQG
SGFIVSADGV ILTNAHVVKD AKEVTVKLTD RREFRAKVLG SDEKTDIAVL KIDAKNLPTL
SLGNTKELKP GEWVLAIGSP FGFENTVTAG VVSAKGRSLP DDSYVPFIQT DVAINPGNSG
GPLINTRGEV VGINSQIYSR SGGYQGVSFA IPIDVAIQVK DQIVATGRAS HARLGVAVQE
VNQTFADSFK LDKPEGALVS NVEKGGPAEQ AGLRSGDVIR KVDGDPVVAS GDLPALIGQK
KPGTKVMLDV WRQGARQELS ARLGDASEKA STVAKSDERA GGGKLGLALR PLQPQEKREA
AVESGLLIED AGGAAALAGV QAGDVLLAVN GTPAKSVEQV REVVNKADKS IALLIQRDGD
RIFVPVRIG
//
