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Desampylase (EC 3.4.19.15) (HvJAMM1)

 JAMM1_HALVD             Reviewed;         139 AA.
D4GTS4;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
28-FEB-2018, entry version 50.
RecName: Full=Desampylase;
EC=3.4.19.15 {ECO:0000269|PubMed:22970855};
AltName: Full=HvJAMM1;
OrderedLocusNames=HVO_2505; ORFNames=C498_07813;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE,
REACTION MECHANISM, AND MUTAGENESIS OF GLU-31; HIS-88; HIS-90; ASP-94;
SER-98; ASP-101 AND CYS-115.
STRAIN=DS2 / DS70;
PubMed=22970855; DOI=10.1111/mmi.12038;
Hepowit N.L., Uthandi S., Miranda H.V., Toniutti M., Prunetti L.,
Olivarez O., De Vera I.M., Fanucci G.E., Chen S., Maupin-Furlow J.A.;
"Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-
like small archaeal modifier proteins (SAMPs) from protein-
conjugates.";
Mol. Microbiol. 86:971-987(2012).
[4]
FUNCTION.
STRAIN=DS2 / DS70;
PubMed=24097257; DOI=10.1074/mcp.M113.029652;
Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J.,
Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L.,
Maupin-Furlow J.A.;
"Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a
UbaA-dependent mechanism.";
Mol. Cell. Proteomics 13:220-239(2014).
-!- FUNCTION: Metalloprotease that displays desampylase (DSAMP)
activity, cleaving ubiquitin-like small archaeal modifier proteins
(SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and
linear-linked). Thus, likely regulates sampylation and the pools
of "free" SAMP available for protein modification. Functions as a
specific and not a general protease since it is unable to
hydrolyze a variety of unmodified proteins otherwise hydrolyzed by
proteinase K. {ECO:0000269|PubMed:22970855,
ECO:0000269|PubMed:24097257}.
-!- CATALYTIC ACTIVITY: An N(6)-[small archaeal modifier protein]-
[protein]-L-lysine + H(2)O = a [protein]-L-lysine + a [small
archaeal modifier protein]. {ECO:0000269|PubMed:22970855}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:22970855};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22970855};
-!- ENZYME REGULATION: Inhibited by EDTA and N-ethylmaleimide (NEM) in
vitro. {ECO:0000269|PubMed:22970855}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7-10. Displays little to no activity at low pH (pH
6.5 and below). {ECO:0000269|PubMed:22970855};
Temperature dependence:
Optimum temperature is 40-50 degrees Celsius. Is active over a
wide range of temperature (20-60 degrees Celsius). However, the
enzyme is not active at 70 degrees Celsius.
{ECO:0000269|PubMed:22970855};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22970855}.
-!- MISCELLANEOUS: Is optimally active at NaCl concentrations of 0.7-2
M, and displays little to no activity at low concentrations of
salt (150 mM NaCl).
-!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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EMBL; CP001956; ADE04294.1; -; Genomic_DNA.
EMBL; AOHU01000045; ELY32652.1; -; Genomic_DNA.
RefSeq; WP_004042475.1; NZ_AOHU01000045.1.
ProteinModelPortal; D4GTS4; -.
SMR; D4GTS4; -.
STRING; 309800.HVO_2505; -.
MEROPS; M67.009; -.
EnsemblBacteria; ADE04294; ADE04294; HVO_2505.
EnsemblBacteria; ELY32652; ELY32652; C498_07813.
GeneID; 8924939; -.
KEGG; hvo:HVO_2505; -.
PATRIC; fig|309800.29.peg.1519; -.
eggNOG; arCOG01138; Archaea.
eggNOG; COG1310; LUCA.
HOGENOM; HOG000009901; -.
KO; K20110; -.
OMA; VGIFHSH; -.
OrthoDB; POG093Z0DIN; -.
BioCyc; HVOL309800:GCOK-2498-MONOMER; -.
BioCyc; MetaCyc:MONOMER-20240; -.
Proteomes; UP000008243; Chromosome.
Proteomes; UP000011532; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
InterPro; IPR028090; JAB_dom_prok.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
Pfam; PF14464; Prok-JAB; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Metal-binding; Metalloprotease;
Protease; Reference proteome; Zinc.
CHAIN 1 139 Desampylase.
/FTId=PRO_0000428938.
DOMAIN 6 139 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOTIF 88 101 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
ACT_SITE 31 31 Proton donor/acceptor.
{ECO:0000305|PubMed:22970855}.
METAL 88 88 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 90 90 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 101 101 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
SITE 98 98 Transition state stabilizer.
{ECO:0000305}.
MUTAGEN 31 31 E->D: Loss of catalytic activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 88 88 H->N: Loss of catalytic activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 90 90 H->Q: Loss of catalytic activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 94 94 D->N: Retains desampylating activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 98 98 S->A: Loss of catalytic activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 101 101 D->E: Loss of catalytic activity.
{ECO:0000269|PubMed:22970855}.
MUTAGEN 115 115 C->S: Retains desampylating activity.
{ECO:0000269|PubMed:22970855}.
SEQUENCE 139 AA; 14739 MW; 432D44455ADF0568 CRC64;
MTSSRLSLAA DARDSILSHA REGAAGDPPA EVCGVLAGDS DARTVTAAHP VSNVAAEPRV
AYELDPEETV SILEAIESAG DDAVGFYHSH PESDPVPSAT DRERASWPGY VYLICSPDGR
MTAHEWTGDE FRELSVAVE


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