ID   TLDD_SACS2              Reviewed;         443 AA.
AC   Q7LXP6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Zinc metalloprotease TldD homolog;
DE            EC=3.4.-.-;
GN   Name=tldD; OrderedLocusNames=SSO0660;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
RP   HIS-228; GLU-229; HIS-233 AND CYS-416.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=22950735; DOI=10.1042/bsr20120074;
RA   Hu Y., Peng N., Han W., Mei Y., Chen Z., Feng X., Liang Y.X., She Q.;
RT   "An archaeal protein evolutionarily conserved in prokaryotes is a zinc-
RT   dependent metalloprotease.";
RL   Biosci. Rep. 32:609-618(2012).
CC   -!- FUNCTION: Zinc metalloprotease. Able to degrade azocasein in vitro.
CC       {ECO:0000269|PubMed:22950735}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:22950735};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:22950735};
CC       Temperature dependence:
CC         Optimum temperature is 55-65 degrees Celsius.
CC         {ECO:0000269|PubMed:22950735};
CC   -!- SUBUNIT: Homodimer.
CC   -!- DOMAIN: The HEAIGH motif probably functions as the active center of the
CC       metalloprotease. {ECO:0000269|PubMed:22950735}.
CC   -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR   EMBL; AE006641; AAK40965.1; -; Genomic_DNA.
DR   PIR; F90213; F90213.
DR   RefSeq; WP_009991202.1; NC_002754.1.
DR   AlphaFoldDB; Q7LXP6; -.
DR   SMR; Q7LXP6; -.
DR   STRING; 273057.SSO0660; -.
DR   EnsemblBacteria; AAK40965; AAK40965; SSO0660.
DR   GeneID; 44129657; -.
DR   KEGG; sso:SSO0660; -.
DR   PATRIC; fig|273057.12.peg.662; -.
DR   eggNOG; arCOG00321; Archaea.
DR   HOGENOM; CLU_026425_1_2_2; -.
DR   InParanoid; Q7LXP6; -.
DR   OMA; TDFWGSM; -.
DR   PhylomeDB; Q7LXP6; -.
DR   BRENDA; 3.4.24.B29; 6163.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   Gene3D; 3.30.2290.10; -; 1.
DR   InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR   InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR   InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR   InterPro; IPR025502; TldD.
DR   InterPro; IPR035068; TldD/PmbA_N.
DR   InterPro; IPR036059; TldD/PmbA_sf.
DR   Pfam; PF01523; PmbA_TldD; 1.
DR   Pfam; PF19289; PmbA_TldD_C; 1.
DR   Pfam; PF19290; PmbA_TldD_M; 1.
DR   PIRSF; PIRSF004919; TldD; 1.
DR   SUPFAM; SSF111283; SSF111283; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metalloprotease; Protease; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Zinc metalloprotease TldD homolog"
FT                   /id="PRO_0000429058"
FT   MOTIF           228..233
FT                   /note="HEAIGH motif"
FT   MUTAGEN         228
FT                   /note="H->F: Abolishes metalloprotease activity. Does not
FT                   affect homodimerization."
FT                   /evidence="ECO:0000269|PubMed:22950735"
FT   MUTAGEN         229
FT                   /note="E->D: Abolishes metalloprotease activity. Does not
FT                   affect homodimerization."
FT                   /evidence="ECO:0000269|PubMed:22950735"
FT   MUTAGEN         233
FT                   /note="H->Y: Abolishes metalloprotease activity. Does not
FT                   affect homodimerization."
FT                   /evidence="ECO:0000269|PubMed:22950735"
FT   MUTAGEN         416
FT                   /note="C->G: Abolishes metalloprotease activity and
FT                   homodimerization."
FT                   /evidence="ECO:0000269|PubMed:22950735"
SQ   SEQUENCE   443 AA;  49882 MW;  34D565FE315CAF03 CRC64;
     MFKYIKKAEE LGASFADIRY ERVIANEVTI TEDRKYVSHG VDEGYSIRVI YNRNWGFKAT
     DKITENEIED TINHIYGDER VNIVYLPSKH DTIKIGKDIN KNEEEKINDL HKVASQVNTL
     HPSIKSYSIK YYDEIFHKEY YSSEDREIIA DGSSSSLSIL VVAREGDVTV EVSEILSTQM
     GYIFDVFDIN QVLANLQKRI INQLKGSTPK AGEYPVILAP EVVGIFTHEA IGHLSEADVT
     LNGSLYKLRN KRIGDEFLNI SDLPAMDHPQ SSLVYYDDEG VEGREVKIIE NGILKEFMTD
     RYYSAYLGQP PTGNARAQSY RNFSLIRMRN TYMKPGDASL NELFEGIKEG YYLVSPIGGE
     TSSNGTFQFA IQEGYRVENS EIKEPLRNIG ISGNTISTLN AIEMISKDFG MSSGFCEKNG
     QTVQVSNGGP HIKVKKLKVG GYV