ID   A0A075LIX1_9BACI        Unreviewed;       496 AA.
AC   A0A075LIX1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=GZ22_08150 {ECO:0000313|EMBL:AIF66610.1};
OS   Terribacillus goriensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX   NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF66610.1, ECO:0000313|Proteomes:UP000027980};
RN   [1] {ECO:0000313|EMBL:AIF66610.1, ECO:0000313|Proteomes:UP000027980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP602 {ECO:0000313|EMBL:AIF66610.1,
RC   ECO:0000313|Proteomes:UP000027980};
RA   Wang Y., Lu P., Zhang L.;
RT   "Complete genome sequence of a moderately halophilic bacterium
RT   Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT   Tianmu mountain in China.";
RL   Submitted (JUL-2014) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP008876; AIF66610.1; -; Genomic_DNA.
DR   RefSeq; WP_038560828.1; NZ_CP008876.1.
DR   AlphaFoldDB; A0A075LIX1; -.
DR   MEROPS; M32.006; -.
DR   KEGG; tap:GZ22_08150; -.
DR   HOGENOM; CLU_032916_1_1_9; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000027980; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000027980};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        262
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   496 AA;  57278 MW;  9A76895890605481 CRC64;
     MSDATQQYWD LIKEQKAYEE AIALMHWDLR TKAPKAGMEY RAEAISYLSQ QSHRLSTSDK
     LKELIDELKP IAEDEILIKS LAESEKEYDR NKKIPEAEFK AYIMLQSKAE SVWGEAREKG
     DFSLLQPYLE ELVTYKKKFA SYWNAEQHAY DVLLDMYEPG VTMETLDEVF PALRNSLTNL
     LDQIKQSNVK PDTSVLQTHF SKEQQKAFTV SVLEKMGYDF EAGRLDDTIH PFEITLNPKD
     VRITTRYDEQ DFRMAVFGTI HEGGHALYEQ NIAEKLAATP LASGTSMGIH ESQSLFWENF
     VARSEAFWKG HFEEFKTYAP ASLQEIDFNT FYQAVNEVKA SFIRIEADEL TYALHIMIRY
     ELEKALFKDE ITVKDLPEIW NSKMEEYLGI VPESDAQGVL QDIHWSGGDF GYFPSYALGY
     MYAAQFHAKM QESLDIDNLI EKGDFSPIKA WLTDQIHQYG KAKKPLELLQ DVTGEGLNAN
     YLVSYLTEKY SKIYQL
//