ID Q01UD7_SOLUE Unreviewed; 492 AA.
AC Q01UD7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:ABJ86733.1};
DE Flags: Precursor;
GN OrderedLocusNames=Acid_5786 {ECO:0000313|EMBL:ABJ86733.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ86733.1};
RN [1] {ECO:0000313|EMBL:ABJ86733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ86733.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP000473; ABJ86733.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01UD7; -.
DR STRING; 234267.Acid_5786; -.
DR KEGG; sus:Acid_5786; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_0; -.
DR InParanoid; Q01UD7; -.
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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABJ86733.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..492
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004162674"
FT DOMAIN 276..340
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 383..492
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 492 AA; 51038 MW; 55B73153B98C068B CRC64;
MSTRTMLIAP AVVLVALAAC GRQTSSSSKN SANREETSSS AIVSRPGPPL SYADVVDHAS
PAVVTIRSER RVRAPEQFPF AEDPSFRQFF GNPLPGRGGQ SAPSQVEHAL GSGVIVRADG
HILTNHHVVD GAEDIKVDLN DHRTLSAKVV GVDPPSDLAV LKIDAQDLPV LALADSDRVR
VGDICLAVGN PLGVGQTVTA GIISARSRST DLSTGSFEDF LQTDAPINQG NSGGALINTN
AALIGINSQI LSPTGGNIGI GFAIPSNLAK NVMDQLITTG KVHRGQLGVG VQPLTSDLAS
GLGLKEVRGV LVNLVKPGSP ADRAGIRNGD VITAIDGHPV DEPNALRNRV ATTAPDSQAK
LSFIRDGKEQ QVTVKLGELT AESAAMERPN GMPGNAPTDR RLGVSVEPLS PALAQELGVR
RDMQGLAVRD VQPDGPAARA GVQPGDVIIA LNRQAVRSAA DVAAALRSAS SRPSLLLINR
AGQNVFLTVS PQ
//
