ID A0A0P1ET59_9RHOB Unreviewed; 491 AA.
AC A0A0P1ET59;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=SHM7688_03222 {ECO:0000313|EMBL:CUH53761.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH53761.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH53761.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH53761.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; CYPW01000027; CUH53761.1; -; Genomic_DNA.
DR RefSeq; WP_058240887.1; NZ_FOMU01000002.1.
DR AlphaFoldDB; A0A0P1ET59; -.
DR STRING; 321267.SHM7688_03222; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000054823; 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:CUH53761.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:CUH53761.1};
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:UP000054823};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 257
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 491 AA; 53665 MW; 0A13B28144D7317E CRC64;
MSAYEQLMAF EHTTQALGQV AGRLGWDQEA IMPKGAAGQR AEEMAAMESV LHARRIDPKV
GEWLAAIDTA QLDEVAKAHV RHIAKTYART SKVPADLAAE IAKVTSRSQG IWAQARSDED
VAGFLPTLQE VVNLKRQEGQ ALAAGGDVYD AMVDDYEPEM TAAEIAAMFD AMRPRLVALR
AAVLAAEAPQ KLSGHYPADK QMALTAKLAA SFGYNFDHGR IDCVTHPFCS GSGQDVRITT
RTSENDPFNC FYSTIHEVGH AAYEQGIDDA YLLTPLGRGV SMGVHESQSR IYENQLGRGR
AYTGWLFEQM KAEFGDFGIE SAEAFYGTVN RVNDGYIRTE ADEVQYNLHI MLRFDLERAL
MLGDLAVNDL EAAWNDRFKA DFGYAVDRPS HGVLQDVHWS VGLFGYFPTY SLGNVYAGCL
NEALRAAVPG LDAQLAQGDT SAATGWLREN LQRHGGLREP AATIEHATGK APSGAPLLDY
LEAKFGEIYG L
//
