Y392_METJA
ID Y392_METJA Reviewed; 339 AA.
AC Q57837;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc metalloprotease MJ0392;
DE EC=3.4.24.-;
DE AltName: Full=MjS2P;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2-type intramembrane protease;
GN OrderedLocusNames=MJ0392;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-224, FUNCTION AS A PROTEASE,
RP ACTIVITY REGULATION, COFACTOR, SUBUNIT, ACTIVE SITE, AND ZINC-BINDING
RP SITES.
RX PubMed=18063795; DOI=10.1126/science.1150755;
RA Feng L., Yan H., Wu Z., Yan N., Wang Z., Jeffrey P.D., Shi Y.;
RT "Structure of a site-2 protease family intramembrane metalloprotease.";
RL Science 318:1608-1612(2007).
CC -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves
CC type-2 transmembrane proteins within their membrane-spanning domains;
CC its endogenous substrate is unknown. Regulated intramembrane
CC proteolysis (RIP) occurs when an extracytoplasmic signal triggers a
CC concerted proteolytic cascade to transmit information and elicit
CC cellular responses. A membrane-spanning regulatory substrate protein is
CC first cut extracytoplasmically (site-1 protease, S1P), then within the
CC membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating the
CC effector protein. Possible signals, S1P and substrates are unknown in
CC this organism. {ECO:0000269|PubMed:18063795}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18063795};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18063795};
CC -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline.
CC {ECO:0000269|PubMed:18063795}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:18063795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; L77117; AAB98382.1; -; Genomic_DNA.
DR PIR; H64348; H64348.
DR RefSeq; WP_010869891.1; NC_000909.1.
DR PDB; 3B4R; X-ray; 3.30 A; A/B=1-224.
DR PDBsum; 3B4R; -.
DR AlphaFoldDB; Q57837; -.
DR SMR; Q57837; -.
DR STRING; 243232.MJ_0392; -.
DR MEROPS; M50.006; -.
DR EnsemblBacteria; AAB98382; AAB98382; MJ_0392.
DR GeneID; 1451249; -.
DR KEGG; mja:MJ_0392; -.
DR eggNOG; arCOG00607; Archaea.
DR HOGENOM; CLU_037123_1_1_2; -.
DR InParanoid; Q57837; -.
DR OMA; IELHITF; -.
DR OrthoDB; 51079at2157; -.
DR PhylomeDB; Q57837; -.
DR BRENDA; 3.4.24.85; 3260.
DR EvolutionaryTrace; Q57837; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF02163; Peptidase_M50; 2.
DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CBS domain; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..339
FT /note="Zinc metalloprotease MJ0392"
FT /id="PRO_0000088480"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 226..281
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 281..335
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT ACT_SITE 55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:18063795"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3B4R"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 38..63
FT /evidence="ECO:0007829|PDB:3B4R"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3B4R"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3B4R"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 91..112
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:3B4R"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 163..187
FT /evidence="ECO:0007829|PDB:3B4R"
FT HELIX 191..218
FT /evidence="ECO:0007829|PDB:3B4R"
SQ SEQUENCE 339 AA; 37965 MW; A56EB35F186A6457 CRC64;
MNYSIRLFKI MGIPIELHIT FILFLVVIIG LSIMNNSIFW AVLFILLFVS VVLHELGHSY
VAKKYGVKIE KILLLPIGGV AMMDKIPKEG ELRIGIAGPL VSFIIGIVLL IVSQFFDINI
NGYPLLYTLS LLNLMLGGFN LIPAFPMDGG RILRAILSKK YGYLKSTKIA ANIGKSLALI
MLLFGLLSMN IILILVSLFV YFGAEQESRV VEVETIFKNI KAKDIMTPNP VYVTPDMSIE
EFLDFMLKHK YFGYPVVENG KLVGCIGIGN IHKKEGTVRD YMEKPVVVSE DTDIKEILRK
MANTDRVFVV EGGKLKGIIS KTDILRAMSI LELKEELKD
