ID A4YF23_METS5 Unreviewed; 1267 AA.
AC A4YF23;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Physarolisin II, Serine peptidase, MEROPS family S53 {ECO:0000313|EMBL:ABP95025.1};
GN OrderedLocusNames=Msed_0851 {ECO:0000313|EMBL:ABP95025.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP95025.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP95025.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP000682; ABP95025.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YF23; -.
DR STRING; 399549.Msed_0851; -.
DR KEGG; mse:Msed_0851; -.
DR eggNOG; arCOG03665; Archaea.
DR HOGENOM; CLU_006754_0_0_2; -.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR017001; Pept_S53_physarolisin-II_arc.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF17957; Big_7; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR PIRSF; PIRSF032623; Peptidase_SSO2181_prd; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1247..1264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..570
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 1267 AA; 135692 MW; 73FDE5C1E826D7A1 CRC64;
MGKTFLAQLT LYLFIFSVVT PALISVANTG TLVHETLSTR LPSFKETNLS GNTPVIASIY
IPLRNLNLLY YYAEQVSNPG SPLYHKFLSP SQVKNLFYPS AEFSSVMNYL ASHHVHVMFT
AADSVIVVQG TASQLSQVLG IHYVLMSNGT TYYYTAMGTP KVPGIVISSN VSALFFSHPS
TLFTQSDVNK LRETVNQPNL TAPIEAYKLT ELRGVYNVSS LISKGVNGTN YTVGILDFYG
DPYIQQQLAY FDKIYNVPAP PNFSIIPIGP YDPNLGITQG WAGEISLDVE SAHAMAPGAN
IVLYIANGNL PLSSVIAEIV SQDKVDTLSQ SFSIPDEFIP EFSGSLFYQC VVLTDQYYAM
GNAEGITFLA SSGDGGGSGY SAGPLGSVGY PASSPFVTAM GGTTTYITFG GFSFNVTAWS
NYGFVPPGVN YGGSTGGISQ VEPKPYYQWG LTTPKGFPNG KEIPDISANA DVYPGIYIVC
PGNVTAISGG TSEASPLTAG LLTLVMQYTH SKLGNINPDL YYLAKADYQK AFYPITFGYN
IPWVASYGYN LVTGWGQLNV GEFASLVKDV PSSLSIMVNV SNTTILPGQT LGVKANVTLN
GQAVNSGSFY VTLETVSGNV TTVKLNDEGS GIWSASLGVP ENDTGITFVT VWGESNGTSG
YGIVETYSGY FVQFLFPAPY QVCWTGSGIN VVVNVTSPSG GIAPNTTVLN LNVYSYNVTN
NSFTLVNQTS LTFNPVFNAW SGMIQGNFPA GPLLLQVVNA YGYDAIFNGI GLNSFFILSP
TIAEPGTVYP GQDIIIEGGL TPPTNLVSSA PRTASDLMTG SNVTAELLYN GQVISKTQVL
YTGTTYLGYL RVPENASPGL YTILLFASYD SYTLNETIPG FYYGQIYVGS RVVTPLNFSN
TYVIQGSTLY IYSNITANGK VVKYGMFSAT VFPTLLTQEY SLISTVLEVP LWYNSTSGLW
TGNVTLPSTL SLGNLTYLGN SYFAEPFKVL VTGVSAYGGV TSTNVSNSRE FFVEPYTLIT
NDPSYTAVQT YDSAFQNDTL TVNGNLVNDL FLGNNTIINS HVTITLSNVT GTLILRNTQA
TLVNVLANKL VLINSTVRLI DSQVQDLVAL SSVVSPIQTR ITSITPGPPI IQLGIAPYQN
ITGNVTISIT VQGQDVEQVL VYLDGQLLAS FQGNGTHEVN LDTLKYADGT HEISVTANQA
DGLNSTVTTN VVFENQLQSV SQKVSNLNET LTQGISTAHS TANVGEIVAI VALILAIVGI
ALDFRRR
//
