ID A0A0S2DH99_LYSEN Unreviewed; 551 AA.
AC A0A0S2DH99;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:QCW26481.1};
DE SubName: Full=Subtilisin N-terminal region/peptidase, families S8 and S53 {ECO:0000313|EMBL:ALN57985.1};
GN ORFNames=FE772_13225 {ECO:0000313|EMBL:QCW26481.1}, GLE_2637
GN {ECO:0000313|EMBL:ALN57985.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN57985.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN57985.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN57985.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW26481.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW26481.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP013140; ALN57985.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW26481.1; -; Genomic_DNA.
DR RefSeq; WP_057947695.1; NZ_CP040656.1.
DR AlphaFoldDB; A0A0S2DH99; -.
DR STRING; 69.GLE_2637; -.
DR KEGG; lez:GLE_2637; -.
DR PATRIC; fig|69.6.peg.2596; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..551
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036001677"
FT DOMAIN 155..361
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 388..460
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 472..537
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 489
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 551 AA; 56044 MW; 56E5D87F88E00E17 CRC64;
MKQSKLMCAL GLALAATTLS TAAMAQEGPN PNRVWVKFKS GAGVSANAAN ARSGLAAPAN
LGQRIQALRG KLSAAKAGDA ELNYQFDRSN TAVMTLSSPE AVKALRANPD VESVEIDQPR
YLQAQSVPYG IDQVQARNVW DANRDGVLDT GAANGSGIKV CIIDSGLNKG HEDFAGMTIT
GYPTGWDTDT CGHGTHVAGT IAAANNNVGV VGVSPGKVSL HIVKIFGSNG YNGSDHGQCS
WTYSSTLADA AQRCQAAGAK VINMSLGGPS ASTAERTAFQ TVADAGVLSI AAAGNDGDSS
QSYPAGYASV VSVAAVDSSN VKADFSQFTP KVELAAPGVD VLSTYPLKND PLVVGTSSFA
AIPVAGSKQA TASAGWVNGG LCQTSSSTWR NKIVVCQRGT NTFVDKITKA KSGRAAGVVI
YNNVDGPLAI GLYTGTAPNL SATTTTLPAV GISKVDGEYL VANLAGKTAT VDATPSVANS
AYETMSGTSM ATPHVAGAAA VVWSAKPTAT AQQVRDALDA TALDIDAAGR DNNTGWGLVQ
IPAAIAELQS Q
//
