ID   JAMM2_HALVD             Reviewed;         161 AA.
AC   D4GVJ3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable metalloprotease HVO_1016;
DE   AltName: Full=HvJAMM2;
GN   OrderedLocusNames=HVO_1016; ORFNames=C498_13679;
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, AND SUBUNIT.
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).
CC   -!- FUNCTION: Probable metalloprotease. Does not hydrolyze SAMP1- and
CC       SAMP2-protein conjugates, diglycine-AMC, Ub-AMC, hemoglobin, cytochrome
CC       c, carbonic anhydrase, creatinine phosphokinase, beta-amylase and
CC       bovine serum albumin. {ECO:0000269|PubMed:22970855}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:22970855}.
CC   -!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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DR   EMBL; CP001956; ADE03305.1; -; Genomic_DNA.
DR   EMBL; AOHU01000092; ELY27597.1; -; Genomic_DNA.
DR   RefSeq; WP_004043926.1; NZ_AOHU01000092.1.
DR   AlphaFoldDB; D4GVJ3; -.
DR   SMR; D4GVJ3; -.
DR   STRING; 309800.C498_13679; -.
DR   EnsemblBacteria; ADE03305; ADE03305; HVO_1016.
DR   EnsemblBacteria; ELY27597; ELY27597; C498_13679.
DR   GeneID; 8926558; -.
DR   KEGG; hvo:HVO_1016; -.
DR   PATRIC; fig|309800.29.peg.2628; -.
DR   eggNOG; arCOG01139; Archaea.
DR   HOGENOM; CLU_116578_0_0_2; -.
DR   OMA; HPNEYMG; -.
DR   OrthoDB; 118690at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR037518; MPN.
DR   Pfam; PF14464; Prok-JAB; 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..161
FT                   /note="Probable metalloprotease HVO_1016"
FT                   /id="PRO_0000428939"
FT   DOMAIN          10..131
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           87..100
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   ACT_SITE        31
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   SITE            97
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   161 AA;  17677 MW;  00C1A5F402E03F9F CRC64;
     MRLFRSREVV GIAADALDFA LEASAETHPN EYMGLLRGEE ARRVGVDRDG YVVTDVLIIP
     GTVSDPYSAT VRNDLVPNDF HAVGSIHSHP NGVLRPSDAD LDTFGSGRVH IIIGSPYGPD
     DWEAFDQSGE VRDLDVLDAD LSDPESFFDF TQDDIDAELD R