JAMM1_THET2
ID JAMM1_THET2 Reviewed; 148 AA.
AC Q72IJ9;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable TtuB-protein conjugate cleaving protease {ECO:0000305|PubMed:22467871};
DE EC=3.4.19.- {ECO:0000305|PubMed:22467871};
GN OrderedLocusNames=TT_C1133 {ECO:0000312|EMBL:AAS81475.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-47 AND
RP 101-HIS--HIS-103.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=22467871; DOI=10.1074/jbc.m112.359844;
RA Shigi N.;
RT "Posttranslational modification of cellular proteins by a ubiquitin-like
RT protein in bacteria.";
RL J. Biol. Chem. 287:17568-17577(2012).
CC -!- FUNCTION: Probable metalloprotease that cleaves the ubiquitin-like
CC modifier protein TtuB from protein conjugates, hydrolyzing the
CC isopeptide bond between a lysine residue of the target protein and the
CC C-terminal glycine of the modifier protein. Does not seem to work for
CC all the TtuB conjugates. {ECO:0000305|PubMed:22467871}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:D4GTS4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:D4GTS4};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show alteration of TtuB
CC conjugation to TtuC and TtuA and about 50% decrease in 5-methyl-2-
CC thiouridine (m(5)s(2)U or s(2)T) amounts in tRNA.
CC {ECO:0000269|PubMed:22467871}.
CC -!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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DR EMBL; AE017221; AAS81475.1; -; Genomic_DNA.
DR AlphaFoldDB; Q72IJ9; -.
DR SMR; Q72IJ9; -.
DR STRING; 262724.TT_C1133; -.
DR EnsemblBacteria; AAS81475; AAS81475; TT_C1133.
DR KEGG; tth:TT_C1133; -.
DR eggNOG; COG1310; Bacteria.
DR HOGENOM; CLU_116765_2_0_0; -.
DR OMA; IGHYHSH; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028090; JAB_dom_prok.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR Pfam; PF14464; Prok-JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..148
FT /note="Probable TtuB-protein conjugate cleaving protease"
FT /id="PRO_0000442739"
FT DOMAIN 22..148
FT /note="MPN"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT MOTIF 101..114
FT /note="JAMM motif"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4,
FT ECO:0000305|PubMed:22467871"
FT ACT_SITE 47
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT SITE 111
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT MUTAGEN 47
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22467871"
FT MUTAGEN 101..103
FT /note="HSH->ASA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22467871"
SQ SEQUENCE 148 AA; 16032 MW; E59A366A7CB4EA17 CRC64;
MAPPSVPIVY AGGRGGCPGG YHGLVLYVPR GLLEETRAHL LREAPKEGVG LWAGRREVER
VIPLPNVHPS PLTAYLADPL ALLKALKALE REGLSLLAIY HSHPKGPALP SPRDIKEARW
RVPYVIFGTD GVRAFLLPEG QEVALVVL
