ID A0A1H7MVF4_9GAMM Unreviewed; 620 AA.
AC A0A1H7MVF4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:SEL14665.1};
GN ORFNames=SAMN05428989_1546 {ECO:0000313|EMBL:SEL14665.1};
OS Pseudoxanthomonas sp. GM95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1881043 {ECO:0000313|EMBL:SEL14665.1, ECO:0000313|Proteomes:UP000199164};
RN [1] {ECO:0000313|Proteomes:UP000199164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM95 {ECO:0000313|Proteomes:UP000199164};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOAX01000001; SEL14665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7MVF4; -.
DR STRING; 1881043.SAMN05428989_1546; -.
DR Proteomes; UP000199164; 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; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011714645"
FT DOMAIN 180..476
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 540..605
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 620 AA; 63165 MW; 5FA29CD41A1E4FA0 CRC64;
MNKLNNVAAM VLAAGCALAV HPSAHAAQTV LAVKPLNVNQ ALQQSEDTDR IVVRYKSASL
SSASKLSAVT GAAIRAGILQ PATRAVAGAA SSTTLTARRL RTLSIGGEVI QLSRQISPAE
QTTLLTKLRA DSTVETAYVS HRAYAQASDP NDAYWGNYEW TLKSGAGGVN APAAWDTTKG
AGVIVAVLDT GILPLHPDHP VNLLEGYDFI SDAEVSGRAT DDRVAGAIDQ GDWTTDEQCT
TGWKGQQSSW HGTHVAGTIA EATNNTIGMA GLAPDATILP VRVLGHCGGY EDDIADAIVW
ASGGHVEGVP DNQNPAEIIN MSLGGGGACT ERPLYQAAID AAVANGTLVV VAAGNNAADT
KNYSPSSCNN VVTVASTGYS GQMSSSYTNY GTLVDVAAPG GAVTEGNPNG YVWQQGYNGT
TTNTSGGYTY MGMAGTSQAT PHVSASAALV QAALIAAGKA PLTPADLETL LKKTARAFPI
APSSSTPIGS GIVDPVAAIQ SALSGGDTCD SDSADCETGV TPVENKVNLV NLSGTSGSET
VYSFKATAGA ALSVITLGGT GNVDVYVSYG KTPSTSVYDA KSARAGNNET VRIATPVAGT
YYIKLVGASQ YAGVTLSVRQ
//