ID Q1GNV9_SPHAL Unreviewed; 423 AA.
AC Q1GNV9;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:ABF54663.1};
GN OrderedLocusNames=Sala_2958 {ECO:0000313|EMBL:ABF54663.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF54663.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF54663.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP000356; ABF54663.1; -; Genomic_DNA.
DR RefSeq; WP_011543227.1; NC_008048.1.
DR AlphaFoldDB; Q1GNV9; -.
DR STRING; 317655.Sala_2958; -.
DR KEGG; sal:Sala_2958; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_21_0_5; -.
DR OrthoDB; 5405281at2; -.
DR Proteomes; UP000006578; 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:UP000006578};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 185..415
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 423 AA; 42788 MW; F38845B1ABE79443 CRC64;
MRYVIAALLT LCFLSGGVIP RAAGQVALPP VGLPDRGRIL PGLPDLAAEP LTVAEDKLRT
LRLDRIAALV RRHPDAIERD ARGDPAVRGV LVAIGVDTAM VARARAAGFA LIDRERLDSL
GLDIVRFRVP DGRSLARAQK QLARLLPDAE VDVDHIYFAS GPGGALPGAA LVATTGAGGG
AAPLGLIDGG VAAHPSVAGR VEQRGFARGA PTASEHGTAV ASLLVGAGAV QGAAPGRRLL
AADVYGNDPA GGSASAIARA LGWLAARRVA VTTISLVGPD NKLLAAAVAA AQRKGMLIVA
AVGNDGPAAP PAYPASYRGV LAVTGVDARA RVLPEAGRAL HVDFAAPGDA VRAATGPASI
ERLRGTSFAA PLVAGRLALH YPAASIAAIG PAITVLVMEA RDLGRKGRDK IYGHGLICGD
CGR
//
