ID G2DZ99_9GAMM Unreviewed; 475 AA.
AC G2DZ99;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:EGV32126.1};
DE EC=3.4.21.108 {ECO:0000313|EMBL:EGV32126.1};
GN ORFNames=ThidrDRAFT_1362 {ECO:0000313|EMBL:EGV32126.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV32126.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV32126.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV32126.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:EGV32126.1}.
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DR EMBL; AFWT01000008; EGV32126.1; -; Genomic_DNA.
DR RefSeq; WP_007040076.1; NZ_AFWT01000008.1.
DR AlphaFoldDB; G2DZ99; -.
DR STRING; 765913.ThidrDRAFT_1362; -.
DR PATRIC; fig|765913.3.peg.1387; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000004200; 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; 2.
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:SF125; PROTEASE DO-LIKE 14-RELATED; 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, ECO:0000313|EMBL:EGV32126.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EGV32126.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039592891"
FT DOMAIN 266..330
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 389..463
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 475 AA; 50013 MW; DABED8F8E2EE9A2D CRC64;
MRSSPALSLA FIALFCCALA PGMAVSRELP DFTALVAKNG PAVVNISTKQ TTTATTPGLR
GFSLPDLPDD SPLQDFFRHF FGEEGDLPDD NIQARSLGSG FIVSSDGYVL TNSHVVESAD
EIVVRTSDRR EFVATLVGTD KRSDIALLKV DGTNLPTARI GSSKDLQVGE WVLAIGSPFG
FESSATAGIV SAKGRSLPTE NYVPFIQTDV AINPGNSGGP LFNLDGDVVG VNSQIYSRTG
GFMGLSFAIP IDVAMDVVNQ LKTKGRVSRG WLGVLIQDVT RELAESFGMP QPRGALVAQV
LPNSPAEAAD LRPGDVILSF NGRDVVTSST LPPLVGETAV GAEAKLQVLR RGKKVDLSVK
IEELPDEEQA ASPGQAPLEE PANRVGLVVR DLTADQRQQL GLAQGGILVE GVDPGPADDA
GIAPGDVILM FDNQPVANVS GFNQILDAVS PGKPVAVLVQ RGESRMFYAI KVPKS
//
