ID M0EYU5_9EURY Unreviewed; 508 AA.
AC M0EYU5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=C465_03385 {ECO:0000313|EMBL:ELZ51579.1};
OS Halorubrum distributum JCM 9100.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227467 {ECO:0000313|EMBL:ELZ51579.1, ECO:0000313|Proteomes:UP000011526};
RN [1] {ECO:0000313|EMBL:ELZ51579.1, ECO:0000313|Proteomes:UP000011526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9100 {ECO:0000313|EMBL:ELZ51579.1,
RC ECO:0000313|Proteomes:UP000011526};
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:ELZ51579.1}.
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DR EMBL; AOJM01000031; ELZ51579.1; -; Genomic_DNA.
DR RefSeq; WP_004595807.1; NZ_AOJM01000031.1.
DR AlphaFoldDB; M0EYU5; -.
DR PATRIC; fig|1227467.4.peg.621; -.
DR Proteomes; UP000011526; 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:ELZ51579.1}; 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; 57640 MW; 607FDF449F3C85CE CRC64;
MATEAAPDDA ADAPDAYDAL LDRVQRWNAV GSASGVLGWD QQVMMPEGGT PARSKQLSAL
SSVHHDMVTA DETGELLDEL DDADLTDEQA AVVREVRREY ERADAVPVEL VEEISETGSE
ALQAWEEAKA EDDFDEFAPY LEKHVELKRE YAEHIDPDRD PYEVLFEEFE PCLSMERAES
ILTELREALV PMIEEIRESD VELAVDTFEG TFPEDDQEAL SREALELVGY DFDRGRLDVS
SHPFTSGNQF DCRVTTRFDE NDPLGAVGST IHEFGHAQYN LGLPQEHFGT PLGESRDLSV
HESQSRLCEN HVGRSKAFWE EFLPVFQEHF PQTEEATVQD AYEAFNQVYE DNLIRVEADE
LTYHLHIVIR FEIERDLIRG DLDVEDVPEV WNDKYEEYLG IRPDTDSEGC LQDIHWSHGN
FGYFPTYSLG SVMAAQLFEA AEDEIDDLHG KIADGEFGDL HDWLGENVHQ HGSRYETNEL
VVRATGEDFS ADAFLDYVDE KYGELYGI
//
