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
//