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Carboxypeptidase 1 (EC 3.4.17.19)

 A0A0N8K7V6_9RHOB        Unreviewed;       490 AA.
A0A0N8K7V6;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
05-JUL-2017, entry version 10.
RecName: Full=Carboxypeptidase 1 {ECO:0000256|PIRNR:PIRNR006615};
EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
Name=taq {ECO:0000313|EMBL:KPP92801.1};
ORFNames=HLUCCA05_10425 {ECO:0000313|EMBL:KPP92801.1};
Roseibaca calidilacus.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Roseibaca.
NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP92801.1, ECO:0000313|Proteomes:UP000050413};
[1] {ECO:0000313|EMBL:KPP92801.1, ECO:0000313|Proteomes:UP000050413}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HL-91 {ECO:0000313|EMBL:KPP92801.1};
Nelson W.C., Romine M.F., Lindemann S.R.;
"Identification and resolution of microdiversity through metagenomic
sequencing of parallel consortia.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Broad specificity carboxypetidase that releases amino
acids sequentially from the C-terminus, including neutral,
aromatic, polar and basic residues.
{ECO:0000256|PIRNR:PIRNR006615}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
specificity, except for -Pro. {ECO:0000256|PIRNR:PIRNR006615}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-
1};
-!- SIMILARITY: Belongs to the peptidase M32 family.
{ECO:0000256|PIRNR:PIRNR006615}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KPP92801.1}.
-----------------------------------------------------------------------
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EMBL; LJSG01000011; KPP92801.1; -; Genomic_DNA.
RefSeq; WP_072245143.1; NZ_FBYC01000004.1.
EnsemblBacteria; KPP92801; KPP92801; HLUCCA05_10425.
PATRIC; fig|1666912.4.peg.2267; -.
Proteomes; UP000050413; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
CDD; cd06460; M32_Taq; 1.
InterPro; IPR001333; Peptidase_M32_Taq.
Pfam; PF02074; Peptidase_M32; 1.
PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
PRINTS; PR00998; CRBOXYPTASET.
3: Inferred from homology;
Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
ECO:0000313|EMBL:KPP92801.1};
Complete proteome {ECO:0000313|Proteomes:UP000050413};
Hydrolase {ECO:0000256|PIRNR:PIRNR006615,
ECO:0000313|EMBL:KPP92801.1};
Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
ECO:0000256|PIRSR:PIRSR006615-1};
Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
Protease {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:KPP92801.1};
Reference proteome {ECO:0000313|Proteomes:UP000050413};
Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
METAL 254 254 Zinc; catalytic.
{ECO:0000256|PIRSR:PIRSR006615-1}.
METAL 258 258 Zinc; catalytic.
{ECO:0000256|PIRSR:PIRSR006615-1}.
METAL 284 284 Zinc; catalytic.
{ECO:0000256|PIRSR:PIRSR006615-1}.
SEQUENCE 490 AA; 53898 MW; B1C552A8E8F3D589 CRC64;
MSAYAELRAH LRQTAALGEI AGRLGWDQQT VMPRGANDQR AEEMAALEDV LHARRTDPGL
GELLARAEAP DETGAAILRE ARRDYARNTR VPARLASELA RVTALSQTAW EEARAADDVA
AFLPWLEQVV ALRRAEGQAI AQGADAYDAL MQDYEPGTDA AQVAAIFDRM RPRLVDLRDR
ILGAPTPPAL QGHFPQDAQL RLANELAGRF GYDFNRGRID LAVHPFSSGS GADVRITTRV
AEDDPFNCLY STLHEVGHAT YEQNIAPDYA LTPLGHGVSM GVHESQSRIY ENQLGRSRAF
TGWLFGAMQA EFGGLNIDSA DAFHAAVNRV HKGYIRTESD EVQYNLHIML RFDLERALIA
GTLAPADLEE AWNTRFEADF GFKVDRPANG VLQDVHWSVG LFGYFPTYAL GNIYAGCLYQ
ALRLEIPNID AHLSNGDPAP ATAWLADKVQ RHGGLRPSVQ TIAHACSRAR PDEGPLLAYL
DAKFADIYKL


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