ID   A0A0K8MY26_9CHLR        Unreviewed;       501 AA.
AC   A0A0K8MY26;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=LARV_03950 {ECO:0000313|EMBL:GAP16154.1};
OS   Longilinea arvoryzae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Longilinea.
OX   NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP16154.1};
RN   [1] {ECO:0000313|EMBL:GAP16154.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOME-1 {ECO:0000313|EMBL:GAP16154.1};
RA   Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT   "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT   caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT   saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT   Members of the Anaerolineaceae (Chloroflexi).";
RL   Submitted (JUL-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}.
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; DF967973; GAP16154.1; -; Genomic_DNA.
DR   RefSeq; WP_075075527.1; NZ_DF967973.1.
DR   AlphaFoldDB; A0A0K8MY26; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000055060; 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:GAP16154.1}; 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   Reference proteome {ECO:0000313|Proteomes:UP000055060};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        265
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   501 AA;  56522 MW;  77118084340CC046 CRC64;
     MNPQLDELKS RLREISALQN AAALLNWDQL TIMPPGGAEA NGYQQSVLAR IATEKSIDPA
     LGKLIGDLLP YAETLPADSD DACLIRMAKY DFDKMIHVPP EFVGRAYEQI ARTYQVWTEA
     RPENNYAKVM PELEKNLELS RELASYYPNV EHVADPLIED SDPGMKAAEL QRLFAELRAE
     LVPIVKAITS QPLADDACLK QHFPADQQLA LGKRAAAAIG YDFNRGRMDL SPHPFTTRFS
     IGDVRITTRI NENDLGESLF SVIHESGHAL YEQGVNPALE GLPLARGASS GVHESQSRTW
     ENIVGRSLPF WMHFYPELKA NFPGKFDTVS LETFYRAINK VEPSLVRTES DEVTYNLHIM
     IRFDLELAML EGKLALRDLP EAWNERYRSD LGITPPDDRM GCMQDVHWFG GFVGGGFQGY
     TLGNIMSAQF MESALKIHPE IPEEIAAGRF DVLRGWLTEK IYSQGRKFFP TELVRRVTGK
     DLEIAPYMRY LKNKYGALYE L
//