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Database: UniProt
Entry: Q4J9N4_SULAC
LinkDB: Q4J9N4_SULAC
Original site: Q4J9N4_SULAC 
ID   Q4J9N4_SULAC            Unreviewed;      1275 AA.
AC   Q4J9N4;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Conserved protein {ECO:0000313|EMBL:AAY80496.1};
GN   OrderedLocusNames=Saci_1147 {ECO:0000313|EMBL:AAY80496.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY80496.1, ECO:0000313|Proteomes:UP000001018};
RN   [1] {ECO:0000313|EMBL:AAY80496.1, ECO:0000313|Proteomes:UP000001018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
RC   {ECO:0000313|Proteomes:UP000001018};
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP000077; AAY80496.1; -; Genomic_DNA.
DR   RefSeq; WP_011277998.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4J9N4; -.
DR   STRING; 330779.Saci_1147; -.
DR   GeneID; 78441491; -.
DR   KEGG; sai:Saci_1147; -.
DR   PATRIC; fig|330779.12.peg.1110; -.
DR   eggNOG; arCOG03665; Archaea.
DR   HOGENOM; CLU_006754_0_0_2; -.
DR   Proteomes; UP000001018; 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; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR017001; Pept_S53_physarolisin-II_arc.
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; 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:UP000001018};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1248..1272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..546
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   1275 AA;  136913 MW;  08F3B315A095DA8A CRC64;
     MQVKFLIPIS ILLISISGIL SLGISSPSNQ NTFFNSYTNA KLLPSNTLLT LTFFIPPKNL
     NMLYYTAEEV ANHQISPLTP QQIIKEFSQP NKVTSLINFL ESNGFTIYYS SPFAVVATAT
     AGKIDNVFST ELGLFSYNGH VYYKPLTSPS FSLTGIIVGG LDNETAFQPY FMQLNNTTHP
     AFQFSYLGYG PNALRTAYNV TGTGKNVTIA IIDAFGDPLI YQDVKSFDQI YGLPPANLSV
     YAVGPYIPEQ GIATGWDIET ALDVEAAHAM APYAKINLVV SSDSGPTLYA AVDYVVTQKL
     GDVVSMSWGL SENLFAASGF YYFINGQPFP NYPYLDYYFA LGTAEGITFF ASSGDTGAYG
     DSLTTYGGAS FPATSPFVTA VGGTTLYLSS GKAYETAWSV LPQYFEYAGT VSSGGGYSTF
     FPRPWYQDGV INSSFRAVPD VAADANPYTG FNITVLGSEE IIGGTSLASP LWAGMLADII
     SQLGRPIGLL NPILYWIYKN PALYQESFHQ ITLGYNGEFY AKPGYNLVTG LGTPNVGELL
     NAIQQYLKTN NLEISVTTNG TIPWYMYNST VSVIAYITYP NGTIVSQGTF SAYIQTTSGT
     VTTIPLSFNG TDWVGSFNIQ PGMTPNIWSI IVNGSSAGFS GTSSYDIDVG QSINILSPIP
     FPYGPPLSLN TPFGVVAQIY NPDGTPAVNQ TVNVYLLKNG KVVESAVLTP TSQPGEYVGQ
     LALITPAEQG TYILVVNTSY GSAYTYVYFG NIIEGAVYTP INTGFPGVSP GQNITLFAFT
     LTPEGTGQLS SNVSAFIYNQ NGQLVSTVNL TQAPEITLFG VFNFFGLYYA NFTIPSNFTP
     GFYSVIIQSQ ARTGIGVSTG EFFTSFYVSP ASLSYNIKVK GIAYEGQHIK IYANITYTNG
     TEVEYGIFNA IPLPSSIAFK SYLVATNYSV PLQFNSTLGL WEGTFQIPSV LGANSFYLGY
     PPYTLSGPWT VYISGVSANG NPISSGPTYF NVLPYTYLGS KVIITSQNYT SVPLLSSNSL
     SNVYVGNLEL INVNISLNNV VVGNLTVVNS QVGVSSSTLN SLTAKNSKLS IAQSTIGGDP
     DSVAIQLYNS SLILTSVVIA NSTYAFNQVN SNVELNGVSL SNVQHVSTIS PPTISPQFVN
     ITQKISALNL TVSGYNAKIL NVLVNGISTR YSVISSSQNS TTISIPFSSS ALPSGQYTIV
     VMTYNGLPYN VSATVYNAYP QISLSSSLSN ATTSLSSKIS SNASDVAFYR NITIASLIIA
     IISLILVIYL LLRRR
//
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