ID C7NX53_HALMD Unreviewed; 509 AA.
AC C7NX53;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=Hmuk_0281 {ECO:0000313|EMBL:ACV46418.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV46418.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV46418.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
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}.
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DR EMBL; CP001688; ACV46418.1; -; Genomic_DNA.
DR RefSeq; WP_012807811.1; NC_013202.1.
DR AlphaFoldDB; C7NX53; -.
DR STRING; 485914.Hmuk_0281; -.
DR GeneID; 8409779; -.
DR KEGG; hmu:Hmuk_0281; -.
DR eggNOG; arCOG04247; Archaea.
DR HOGENOM; CLU_032916_1_1_2; -.
DR OrthoDB; 7244at2157; -.
DR Proteomes; UP000001746; Chromosome.
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:ACV46418.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:ACV46418.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 272
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 509 AA; 57555 MW; DDF5A94E92AC3120 CRC64;
MATEADADDA ETPDTYEQFR AHVEQLTYVG DAAGVLQWDQ EVMMPDEGTP ARSKQSAALS
TLSHDLLTDD DVAEWLDELE GSDLDPEREA VVREIRRQHD RAAKVPSDLV QRISEATSNA
LPVWKEAKAE DDFEIYADTL EELVQLKREY AEAIDPDRDP YAVLFEEYEP YLGLDTAEAA
LEDLRDTLVP LIDDIKDSDV TLADPFAGGS YDEASQEDLV RSALDYLGYD WDRGRLDTAP
HPFSTGTQFD ARVTTRFDPE DPLGALSSTI HEFGHATYTL GLPDEHYGTP LGESRDLSVH
ESQSRLWENH VGRSRPFWEG FAPTVEDHLA TSATPREYYE AANTVHPDNC IRVEADELTY
HMHIVLRFEI ERDLIHGDLD VSEVPQVWND KMEEYLGVRP ETDAEGCLQD IHWSHGSFGY
FPTYSLGSVL AAQLFAAAED DIGDLDGQLR DGEFDDLHEW LTDNVHSHGA RYETDDLIEE
ATGEPFTADY FLEYAESKYR DLYDCYSNN
//
