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
//