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Database: UniProt
Entry: F2F720_SOLSS
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ID   F2F720_SOLSS            Unreviewed;       349 AA.
AC   F2F720;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Predicted secreted protein containing a PDZ domain {ECO:0000313|EMBL:BAK17539.1};
GN   OrderedLocusNames=SSIL_3116 {ECO:0000313|EMBL:BAK17539.1};
OS   Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX   NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK17539.1, ECO:0000313|Proteomes:UP000006691};
RN   [1] {ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA   Morohoshi T., Someya N., Ikeda T.;
RT   "Genome sequence of Solibacillus silvestris StLB046.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAK17539.1, ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|EMBL:BAK17539.1,
RC   ECO:0000313|Proteomes:UP000006691};
RX   PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA   Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT   "Complete genome sequence and characterization of the N-acylhomoserine
RT   lactone-degrading gene of the potato leaf-associated Solibacillus
RT   silvestris.";
RL   J. Biosci. Bioeng. 113:20-25(2012).
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DR   EMBL; AP012157; BAK17539.1; -; Genomic_DNA.
DR   RefSeq; WP_014824554.1; NC_018065.1.
DR   AlphaFoldDB; F2F720; -.
DR   STRING; 1002809.SSIL_3116; -.
DR   MEROPS; S16.012; -.
DR   KEGG; siv:SSIL_3116; -.
DR   PATRIC; fig|1002809.3.peg.3145; -.
DR   eggNOG; COG3480; Bacteria.
DR   HOGENOM; CLU_042037_2_0_9; -.
DR   Proteomes; UP000006691; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; NF041438; SepM_fam_S16; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF48; ENDOPEPTIDASE LA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006691};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          100..186
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   349 AA;  38505 MW;  1697CC4CAAE2D4BA CRC64;
     MGNKGKIAFG LFLVILMGLS FYRLDYYITK PGGTYNVSDF LAIQNGDPDD EGSFYMTTVA
     MGQATPLTYA MAAVADYYDI VKLTDVRQEE EDDEEYNVRQ LKYMTDSQFN ATYVAFNRAG
     LDYQVTYKGL YVLNVLAEGA ADGHLKPGDE IVEVDNERID SLETFVTIIT PKVKGDKINL
     VVKRDGKLID ETLEIKEIPG SEGRFGIGIT YSESKSIKTD PKVTVKTEDI GGPSAGLMFT
     LELLNQLIDE DLTKGYEIAG TGEMLEDGTV GRIGGIEKKV VSADKEGVDI FFAPDDEITK
     EMLEYNPSIT SNYEVAAQTA KAINSDIKVV PVKTIDDALN YLDQLQPKN
//
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