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Database: UniProt
Entry: S4XWB8_SORCE
LinkDB: S4XWB8_SORCE
Original site: S4XWB8_SORCE 
ID   S4XWB8_SORCE            Unreviewed;       390 AA.
AC   S4XWB8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:AGP37492.1};
GN   ORFNames=SCE1572_25175 {ECO:0000313|EMBL:AGP37492.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP37492.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP37492.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP37492.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT   milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; CP003969; AGP37492.1; -; Genomic_DNA.
DR   RefSeq; WP_020736955.1; NC_021658.1.
DR   AlphaFoldDB; S4XWB8; -.
DR   STRING; 1254432.SCE1572_25175; -.
DR   KEGG; scu:SCE1572_25175; -.
DR   PATRIC; fig|1254432.3.peg.5716; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_2_0_7; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000014803; 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; 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   Hydrolase {ECO:0000313|EMBL:AGP37492.1};
KW   Protease {ECO:0000313|EMBL:AGP37492.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..390
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004525785"
FT   DOMAIN          280..377
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          23..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  40560 MW;  A84761509E49B6BF CRC64;
     MRHRRLARLP AFLAVAALAA APGCKGKPSP GAPSQSATTA PDAPAAPATS ATLQTMPPPV
     TPPSKNALIE DERNTISVFR EVAPATVFVT QRRLVVDRFW GTAVEVPAGS GTGFVWDADG
     HIVTNFHVVD NAQSLVVQLQ GEKTFPAKLV GVEPRKDIAV LKIDAPKEML KPIQVAPLRE
     PLEVGQKAIA IGNPFGLDHT LTTGIISALG RQVEGAGGVT IRDMIQTDAA INPGNSGGPL
     LDSSGHLIGM NTMIFSKSGT SAGIGFAVPS TTIARVVPQI IRTGKAETVG LGIQLDPARR
     LERRNGIRGV IVMGIVPGGP AEKAGLRGLS EGDRGLTLGD VIVGIDGAPV ADYDALYNAL
     DGKKPGEKVK VDLLRGGQKT TVEVQVELLS
//
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