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
//