JAMM1_HALVD
ID JAMM1_HALVD Reviewed; 139 AA.
AC D4GTS4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Desampylase;
DE EC=3.4.19.15 {ECO:0000269|PubMed:22970855};
DE AltName: Full=HvJAMM1;
GN OrderedLocusNames=HVO_2505; ORFNames=C498_07813;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, REACTION
RP MECHANISM, AND MUTAGENESIS OF GLU-31; HIS-88; HIS-90; ASP-94; SER-98;
RP ASP-101 AND CYS-115.
RC STRAIN=DS2 / DS70;
RX PubMed=22970855; DOI=10.1111/mmi.12038;
RA Hepowit N.L., Uthandi S., Miranda H.V., Toniutti M., Prunetti L.,
RA Olivarez O., De Vera I.M., Fanucci G.E., Chen S., Maupin-Furlow J.A.;
RT "Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like
RT small archaeal modifier proteins (SAMPs) from protein-conjugates.";
RL Mol. Microbiol. 86:971-987(2012).
RN [4]
RP FUNCTION.
RC STRAIN=DS2 / DS70;
RX PubMed=24097257; DOI=10.1074/mcp.m113.029652;
RA Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J.,
RA Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L.,
RA Maupin-Furlow J.A.;
RT "Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-
RT dependent mechanism.";
RL Mol. Cell. Proteomics 13:220-239(2014).
CC -!- FUNCTION: Metalloprotease that displays desampylase (DSAMP) activity,
CC cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2
CC and SAMP3) from protein conjugates (isopeptide- and linear-linked).
CC Thus, likely regulates sampylation and the pools of 'free' SAMP
CC available for protein modification. Functions as a specific and not a
CC general protease since it is unable to hydrolyze a variety of
CC unmodified proteins otherwise hydrolyzed by proteinase K.
CC {ECO:0000269|PubMed:22970855, ECO:0000269|PubMed:24097257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(6)-[small archaeal modifier protein]-[protein]-L-lysine +
CC H2O = a [protein]-L-lysine + a [small archaeal modifier protein].;
CC EC=3.4.19.15; Evidence={ECO:0000269|PubMed:22970855};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22970855};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22970855};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and N-ethylmaleimide (NEM) in
CC vitro. {ECO:0000269|PubMed:22970855}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-10. Displays little to no activity at low pH (pH 6.5
CC and below). {ECO:0000269|PubMed:22970855};
CC Temperature dependence:
CC Optimum temperature is 40-50 degrees Celsius. Is active over a wide
CC range of temperature (20-60 degrees Celsius). However, the enzyme is
CC not active at 70 degrees Celsius. {ECO:0000269|PubMed:22970855};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22970855}.
CC -!- MISCELLANEOUS: Is optimally active at NaCl concentrations of 0.7-2 M,
CC and displays little to no activity at low concentrations of salt (150
CC mM NaCl).
CC -!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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DR EMBL; CP001956; ADE04294.1; -; Genomic_DNA.
DR EMBL; AOHU01000045; ELY32652.1; -; Genomic_DNA.
DR RefSeq; WP_004042475.1; NZ_AOHU01000045.1.
DR AlphaFoldDB; D4GTS4; -.
DR SMR; D4GTS4; -.
DR STRING; 309800.C498_07813; -.
DR MEROPS; M67.012; -.
DR EnsemblBacteria; ADE04294; ADE04294; HVO_2505.
DR EnsemblBacteria; ELY32652; ELY32652; C498_07813.
DR GeneID; 8924939; -.
DR KEGG; hvo:HVO_2505; -.
DR PATRIC; fig|309800.29.peg.1519; -.
DR eggNOG; arCOG01138; Archaea.
DR HOGENOM; CLU_116765_4_2_2; -.
DR OMA; GIFHSHL; -.
DR OrthoDB; 101895at2157; -.
DR BioCyc; MetaCyc:MON-20240; -.
DR BRENDA; 3.4.19.15; 2561.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 InterPro; IPR037518; MPN.
DR Pfam; PF14464; Prok-JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..139
FT /note="Desampylase"
FT /id="PRO_0000428938"
FT DOMAIN 6..139
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 88..101
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT ACT_SITE 31
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:22970855"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT SITE 98
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT MUTAGEN 31
FT /note="E->D: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 88
FT /note="H->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 90
FT /note="H->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 94
FT /note="D->N: Retains desampylating activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 98
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 101
FT /note="D->E: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22970855"
FT MUTAGEN 115
FT /note="C->S: Retains desampylating activity."
FT /evidence="ECO:0000269|PubMed:22970855"
SQ SEQUENCE 139 AA; 14739 MW; 432D44455ADF0568 CRC64;
MTSSRLSLAA DARDSILSHA REGAAGDPPA EVCGVLAGDS DARTVTAAHP VSNVAAEPRV
AYELDPEETV SILEAIESAG DDAVGFYHSH PESDPVPSAT DRERASWPGY VYLICSPDGR
MTAHEWTGDE FRELSVAVE
