ID M0NPF5_9EURY Unreviewed; 508 AA.
AC M0NPF5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=C468_14902 {ECO:0000313|EMBL:EMA59044.1};
OS Halorubrum kocurii JCM 14978.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA59044.1, ECO:0000313|Proteomes:UP000011546};
RN [1] {ECO:0000313|EMBL:EMA59044.1, ECO:0000313|Proteomes:UP000011546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA59044.1,
RC ECO:0000313|Proteomes:UP000011546};
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).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA59044.1}.
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DR EMBL; AOJH01000088; EMA59044.1; -; Genomic_DNA.
DR RefSeq; WP_008849644.1; NZ_AOJH01000088.1.
DR AlphaFoldDB; M0NPF5; -.
DR STRING; 1230456.C468_14902; -.
DR PATRIC; fig|1230456.3.peg.2970; -.
DR OrthoDB; 7244at2157; -.
DR Proteomes; UP000011546; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:EMA59044.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 273
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 508 AA; 57435 MW; 44C9FFCAE37D5039 CRC64;
MATEAATDDA ADAPEAYDAL LDRVRRWNAV GSAAGVLGWD QQVMMPEGGT PARSKQLSTL
SSIRHDMVTD EETGALLDEL ADADLTDEQA AVVREVRRDY ERADAVPVEL VEEISETSTE
ALQAWEEAKA EDDFDEFAPH LEKHVELKRE YAEHIDPDRD PYEVLFEEFE PCLSMDRAEA
ILTELRETLV PMIDAIRESD ADLAVDTFEG AFPEDDQEAL ARETLELVGY DFDRGRLDVS
SHPFTAGNQF DCRVTTRFDE SDPLGAIGST IHEFGHAQYN LGLPREQFGT PLGESRDLSV
HESQSRLWEN HVGRSRAFWE LFLPTFQEHF PETDDATIED AYQAFNQVHE DNLIRVEADE
LTYHLHIVVR FEIERDLVRG DLAVEDVPEV WNDKYEEYLG IRPDTDAEGC LQDIHWSHGN
FGYFPTYSLG SVMAAQLFAA AESEIDDLDG KIAAGEFDDL REWLGENVHR HGSRYETNEL
VKRATGDDFS ADAFTDYVEA KYGDLYGI
//
