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Database: UniProt
Entry: A0A136KX68_9CHLR
LinkDB: A0A136KX68_9CHLR
Original site: A0A136KX68_9CHLR 
ID   A0A136KX68_9CHLR        Unreviewed;       501 AA.
AC   A0A136KX68;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=UZ15_CFX003003164 {ECO:0000313|EMBL:KXK14009.1};
OS   Chloroflexi bacterium OLB15.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK14009.1, ECO:0000313|Proteomes:UP000070332};
RN   [1] {ECO:0000313|EMBL:KXK14009.1, ECO:0000313|Proteomes:UP000070332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB15 {ECO:0000313|EMBL:KXK14009.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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   -!- 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:KXK14009.1}.
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DR   EMBL; LMZS01000171; KXK14009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KX68; -.
DR   PATRIC; fig|1617416.3.peg.3339; -.
DR   Proteomes; UP000070332; 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:KXK14009.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:KXK14009.1};
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   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        266
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
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         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         295
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;  56729 MW;  C83FBF49CA754744 CRC64;
     MSDSLLNELK NRLHEVADLA QAGSVLNWDM ATYMPPKGAP QRGRALATLS KLHHEKFTDP
     AVGHLLDQLE AQLGDRPDDD DDAALVRVTL REYNRAVKVP ASLVGEISEL TSTLYDAWTR
     ARPANDFASL MPMLEREIDL YRQMANCFPG YRHISDPLID FSDYGMSAES IRSIFSELRA
     ELVPIVKAII EQGSADDSPL HQIYPETDQE AFGVEIIKAY GYDFERGRQD RTHHPFMTRF
     SGNDVRITTR FRENALDDGL FSTLHEAGHA LYEQGIDPKF DGTPLGGGTS TGVHESQSRL
     WENIVGRSHG FWSQYYPQLQ VMFPEQLNTV SLEEFYRAIN VAKPSLIRVD ADEVTYNLHV
     MIRFDLELGL MEGSLEVKDL PEIWHSRYAS DLGVTAPDDR DGVLQDVHWY TGIFGYFQGY
     TLGNLMSAQF YDAALRAHPA IPAEIAEGKF DTLRSWLTEN IYRHGSKFTT DELLRRATGE
     GLGIQAWINY IRGKYGEMYK L
//
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