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Database: UniProt
Entry: L0A8W2_CALLD
LinkDB: L0A8W2_CALLD
Original site: L0A8W2_CALLD 
ID   L0A8W2_CALLD            Unreviewed;      1397 AA.
AC   L0A8W2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Putative protease {ECO:0000313|EMBL:AFZ69859.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Calag_0068 {ECO:0000313|EMBL:AFZ69859.1};
OS   Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS   IC-154).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC   Caldisphaera.
OX   NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ69859.1, ECO:0000313|Proteomes:UP000010469};
RN   [1] {ECO:0000313|Proteomes:UP000010469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15908 / JCM 11604 / IC-154
RC   {ECO:0000313|Proteomes:UP000010469};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP003378; AFZ69859.1; -; Genomic_DNA.
DR   RefSeq; WP_015231757.1; NC_019791.1.
DR   STRING; 1056495.Calag_0068; -.
DR   GeneID; 14211328; -.
DR   KEGG; clg:Calag_0068; -.
DR   eggNOG; arCOG03665; Archaea.
DR   HOGENOM; CLU_006754_0_0_2; -.
DR   InParanoid; L0A8W2; -.
DR   OMA; DYYFALG; -.
DR   OrthoDB; 56693at2157; -.
DR   Proteomes; UP000010469; 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:UniProtKB-KW.
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; 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; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 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   Hydrolase {ECO:0000313|EMBL:AFZ69859.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:AFZ69859.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010469};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1369..1392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..599
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   1397 AA;  151012 MW;  F5A7EB3E07E28C05 CRC64;
     MGNILKSFLK LSSIGLIMVF IISAISPLTF ALTNNANNNT YYYGSSLNGT FISDLPSNTM
     ISFSIFLPPR NYNYLIFIAQ QVSNKQMKPL SRNDVLNMFA PSSQEFNEIL NTLKSDGFII
     TYQSPDRFSI MVEAPAYLVE KLFNIKLGLY KSYNGEIYYA PVNTPKIPSF LSNTLIFGLN
     NYTSFVAPHI IAGKIVNKYF VPNASNKLYA LYVKKNQLAG AFTYYTPGDF EGAYNVTNIM
     KYSNKSSIAI IDAYGDPLIY QDIQEFDSMF NLPPANLTVI PIGPYHPSLG ILPGWDIETA
     LDVEAAQSMA PYAHIYLVVA SNPMNALFEA IDYVVSENLA NTVSMSWGST ENTIALTGFY
     TSNPLYTEEQ LNLGYAYADY YFALGSAEGI SFFASSGDNG AYDATPTLYG AVLFPSTSPF
     VTAVGGTSLF VNVTSGYLSS LNSTGTFGYE NAWSVSPLYG TSEVGSTGGY SSLIPKPWYQ
     IGVVNGTFRA VPDVAADANP YTGFVEIVMG SLTVIGGTSL ASPLWAGIAA DIDGYLNTSL
     GLLNPLLYDI YQNKTLYDMA FHQITFGYNG YYSATSGYNL VTGLGSPNAG ILAEAIKDII
     SEPHLEVSVT TMQPGSTYPW YNYNTSFEVV SYITFQNGTS VTTGSFNAYI YTVNGLLEKV
     PLTYNGQYWV ANVTIEPGNP PNTWTIVVNG TSNDLSGLGA TDIDVGVGLA IISPFTAMLY
     PFGPPLFPNT PYPIEVYATL PNGMPDTNLT LNAYLIKNGV TYYSTELVNE GDGTYVGNIF
     LPYPDPQGVY TLLVNSSLGS VYTYEYFGEA IYESFVITPV NDGLPSTSPG ETVTLAALVF
     NPIGLGMYTS NVFANIYNLS GYLVAQIPLT PTASGLQVGS YTIPANLSPG FYNVVFVSSE
     NTSISPLFGY ANQSFLVAPS GLQTTINAVS IAYEGQSIDI YANITYPNGT EVKFGTFTAT
     LIPDQYYSSL LTYSFTVGIP LQYNSTLNEW VGILSLPSLS NPGIFTGLSS LELSGPWSLT
     ISGESAFGHD IVSTPYNIYL EPYTYVGSML LTENNLTSLP MGTQFGNSIT GIYSSELIIE
     NASVTIENSL INNLTIINSK VKVINSKVET ISSKNSKLVL IDDDIGPGSI GVTLTNSNAN
     IINSLFENLQ YAFYQENSTV YLSGFNEYNV TSLSKLPKPS IVSTYPENIT TPISNVIVNV
     TGVNIVPTEV LLNGIPVNFS YKNISGLLEI MIPFNSTELP DGTYTITVVL NNGLLYNVSS
     KIYNNYHLLS QNSLIQYLKN MTSSELSSLS STMTKEYSNL SSEFSSLKIS LSNVNSTLES
     QVSSLNNRLN NVASSLNTTI ASQVSYLERT ISSINSTATS ASKTGSTSYV IGTSGVAVGI
     VGILLGGIAL AMRRVVK
//
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