ID A0A0G3XDT2_9SPHN Unreviewed; 407 AA.
AC A0A0G3XDT2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:AKM08801.1};
GN ORFNames=AB433_00390 {ECO:0000313|EMBL:AKM08801.1}, GGR19_003124
GN {ECO:0000313|EMBL:MBB3991686.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM08801.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM08801.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM08801.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3991686.1, ECO:0000313|Proteomes:UP000536420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102796 {ECO:0000313|EMBL:MBB3991686.1,
RC ECO:0000313|Proteomes:UP000536420};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP011770; AKM08801.1; -; Genomic_DNA.
DR EMBL; JACIEL010000023; MBB3991686.1; -; Genomic_DNA.
DR RefSeq; WP_047819498.1; NZ_JACIEL010000023.1.
DR AlphaFoldDB; A0A0G3XDT2; -.
DR STRING; 1348774.AB433_00390; -.
DR KEGG; cna:AB433_00390; -.
DR PATRIC; fig|1348774.3.peg.91; -.
DR OrthoDB; 5405281at2; -.
DR Proteomes; UP000035287; Chromosome.
DR Proteomes; UP000536420; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05561; Peptidases_S8_4; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000035287};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..407
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033223042"
FT DOMAIN 210..368
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 407 AA; 42320 MW; 5F92388214706B06 CRC64;
MRRISLLIVA ALAVMALPAM AQLRLPPLGI PPLGDVTDTI SDTLEDANAD VARVSEDLLS
IRDNRIAKLL RNHPEALERD SNGDLARRGE LFLLDADPDA LAVARKAGFV IRATEPIDGL
DIELVRLSVP QSLSLAEAED VLRDMLPDAT ISADNLHFPA GGSTASATSV MLASSATSIR
TAVGMIDGAP GNQVRPSSIR GFAQGAPFPS NHGTAIAFLL AFAGVKDIRV ADVYGTDPAG
GNALAIAKAL GWLTKDGAKV ITISLVGPRN ALLERAVDSA QRQGVIIVAA VGNDGPAAPP
AYPASYAGVL AVTAVDGRNR ALIEAGKASH LDYAAPGANL RVRNAKGERA RVRGTSFAVP
LVAARVAAHD GSRSQITVQL DREAVDLGRK GPDDTYGRGL LCSDCRP
//
