ID A0A0N9UTT6_SPHMC Unreviewed; 422 AA.
AC A0A0N9UTT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ALH79334.1};
GN ORFNames=AN936_02805 {ECO:0000313|EMBL:ALH79334.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH79334.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH79334.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH79334.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP012700; ALH79334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N9UTT6; -.
DR KEGG; smag:AN936_02805; -.
DR PATRIC; fig|33050.5.peg.585; -.
DR OrthoDB; 5405281at2; -.
DR Proteomes; UP000058074; Chromosome.
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 InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006039037"
FT DOMAIN 179..413
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 186
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 422 AA; 42535 MW; E3EDB952B4C4F08B CRC64;
MQRTATILAM TALLLAGTTG SLHAQLALPS ARLPGDLPTL PPLADLPAER LAGLGGTLAQ
LRRDRIDSLL RGNRDRIELD ERGEPAVRGT LIASGVDEAM IGAAAKQGFA LIDRERIDGL
DLDIARFRVP GDRSLARARK QLAKLLPEAE VDVDNIYFAS GPGGALPGAA LATAQGSGGA
ALGLIDGGVA AHPSVAGRVE QRGFAKGAPA ASRHGTAVAS LLIGNGAVRG AAPGRHLLAA
DVYGTDPAGG NASAIARALG WLAQNGVAVT TISLVGPDNK LLAAAIARAQ QRGMLIVAAV
GNDGPAAPPA YPAAYRGVFA VTGVDAKGRA LPEAGRALHV DFAAPGDAVL AATGAGSSNR
LRGTSFAAPL VAGRLALRYP VPAIDRIGPA VTALVMEAQD LGKQGRDKIY GHGLICGTCG
GH
//
