ID   Q12RY1_SHEDO            Unreviewed;       358 AA.
AC   Q12RY1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Peptidase S1C, DegS {ECO:0000313|EMBL:ABE53795.1};
GN   OrderedLocusNames=Sden_0503 {ECO:0000313|EMBL:ABE53795.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE53795.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE53795.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
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   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; CP000302; ABE53795.1; -; Genomic_DNA.
DR   RefSeq; WP_011494961.1; NC_007954.1.
DR   AlphaFoldDB; Q12RY1; -.
DR   STRING; 318161.Sden_0503; -.
DR   MEROPS; S01.275; -.
DR   KEGG; sdn:Sden_0503; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_2_6; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000001982; Chromosome.
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; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011783; Pept_S1C_DegS.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; TIGR02038; protease_degS; 1.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001982}.
FT   DOMAIN          270..342
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   ACT_SITE        102
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT   ACT_SITE        132
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
SQ   SEQUENCE   358 AA;  37154 MW;  6B74B359EE26897B CRC64;
     MNIKALLLYL TKAVLFGLVM AAVFLGATSI INGDGFGSNL TGNNHSSKTL SFAAAVRKAA
     PAVVNIYSLS IAEDQPLNSG SLQGLGSGVI MSKEGYILTN YHVIKKADEI VVALQDGRKY
     TSEVVGSDPE TDLTVLKIDG DNLPVVPLNL LTPVQVGDVV LAIGNPYNIG QTITQGIISA
     TGRNGLSSGY LDFLQTDAAI NAGNSGGALI DTDGELVGIN TAAFQVGGEA SGNGISFAIP
     IKLAHSIMGK LIKNGRVIRG AIGVSGEALS PVLAQILNLP NQKGVVVTGV DPTGPAARAQ
     LRARDVIIAY ENEEVPGVEM LMDRIAETPP DSRVTLTIIR EGKVQALPVV IAEKPLPE
//