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Multifunctional CCA protein [Includes: CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl-transferase) (tRNA nucleotidyltransferase) (tRNA-NT); 2'-nucleotidase (EC 3.1.3.-); 2',3'-cyclic phosphodiesterase (EC 3.1.4.-); Phosphatase (EC 3.1.3.-)]

 CCA_ECOLI               Reviewed;         412 AA.
P06961; Q2M9E9;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
10-OCT-2018, entry version 159.
RecName: Full=Multifunctional CCA protein;
Includes:
RecName: Full=CCA-adding enzyme;
EC=2.7.7.72;
AltName: Full=CCA tRNA nucleotidyltransferase;
AltName: Full=tRNA CCA-pyrophosphorylase;
AltName: Full=tRNA adenylyl-/cytidylyl-transferase;
AltName: Full=tRNA nucleotidyltransferase;
AltName: Full=tRNA-NT;
Includes:
RecName: Full=2'-nucleotidase;
EC=3.1.3.-;
Includes:
RecName: Full=2',3'-cyclic phosphodiesterase;
EC=3.1.4.-;
Includes:
RecName: Full=Phosphatase;
EC=3.1.3.-;
Name=cca; OrderedLocusNames=b3056, JW3028;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3009457;
Cudny H., Lupski J.R., Godson G.N., Deutscher M.P.;
"Cloning, sequencing, and species relatedness of the Escherichia coli
cca gene encoding the enzyme tRNA nucleotidyltransferase.";
J. Biol. Chem. 261:6444-6449(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-76, AND MUTAGENESIS OF GLY-70.
PubMed=3533927;
Zhu L.Q., Cudny H., Deutscher M.P.;
"A mutation in Escherichia coli tRNA nucleotidyltransferase that
affects only AMP incorporation is in a sequence often associated with
nucleotide-binding proteins.";
J. Biol. Chem. 261:14875-14877(1986).
[5]
FUNCTION, NUCLEOTIDYLTRANSFERASE ACTIVITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=3516995;
Cudny H., Deutscher M.P.;
"High-level overexpression, rapid purification, and properties of
Escherichia coli tRNA nucleotidyltransferase.";
J. Biol. Chem. 261:6450-6453(1986).
[6]
PHOSPHOHYDROLASE ACTIVITIES, CHARACTERIZATION, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-21; ASP-23;
HIS-255; ASP-256; HIS-305 AND ASP-306.
PubMed=15210699; DOI=10.1074/jbc.M405120200;
Yakunin A.F., Proudfoot M., Kuznetsova E., Savchenko A., Brown G.,
Arrowsmith C.H., Edwards A.M.;
"The HD domain of the Escherichia coli tRNA nucleotidyltransferase has
2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase
activities.";
J. Biol. Chem. 279:36819-36827(2004).
-!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
terminal CCA sequence in tRNAs without using a nucleic acid
template. Adds these three nucleotides in the order of C, C, and A
to the tRNA nucleotide-73, using CTP and ATP as substrates and
producing inorganic pyrophosphate. Also shows highest phosphatase
activity in the presence of Ni(2+) and hydrolyzes pyrophosphate,
canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP
with the production of Pi. Displays a metal-independent
phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and
2',3'-cCMP. Without metal or in the presence of Mg(2+), this
protein hydrolyzes 2',3'-cyclic substrates with the formation of
2'-nucleotides, whereas in the presence of Ni(2+), it also
produces some 3'-nucleotides. These phosphohydrolase activities
are probably involved in the repair of the tRNA 3'-CCA terminus
degraded by intracellular RNases. {ECO:0000269|PubMed:3516995}.
-!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a
3' CCA end + 3 diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Magnesium is required for nucleotidyltransferase activity.;
-!- COFACTOR:
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Note=Nickel for phosphatase activity.;
-!- ACTIVITY REGULATION: Both phosphatase and phosphodiesterase
activities are competitively inhibited by low concentrations of
the E.coli tRNA (10 nM). Cu(2+) stimulates the hydrolysis of
pyrophosphate and ATP and completely inhibits the hydrolysis of
2'-AMP. The phosphodiesterase activity is inhibited by Zn(2+),
Cu(2+) and Co(2+).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.33 mM for ATP (in the tRNA-NT activity assay)
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
KM=0.03 mM for CTP (in the tRNA-NT activity assay)
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
KM=0.015 mM for tRNA-CC {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.02 mM for tRNA-C {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=6.2 mM for pNPP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.10 mM for PPi {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.15 mM for NADP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.19 mM for ADP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.18 mM for ATP (in the phosphatase activity assay)
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
KM=0.53 mM for CDP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.13 mM for CTP (in the phosphatase activity assay)
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
KM=0.76 mM for 2'-AMP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=0.49 mM for 2',3'-cAMP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
KM=1.60 mM for 2',3'-cGMP {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
Vmax=12.4 umol/min/mg enzyme with pNPP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=3.01 umol/min/mg enzyme with PPi as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=17.9 umol/min/mg enzyme with NADP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=1.49 umol/min/mg enzyme with ADP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=4.53 umol/min/mg enzyme with ATP as substrate (in the
phosphatase activity assay) {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
Vmax=5.80 umol/min/mg enzyme with CDP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=4.03 umol/min/mg enzyme with CTP as substrate (in the
phosphatase activity assay) {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
Vmax=3.71 umol/min/mg enzyme with 2'-AMP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=3.21 umol/min/mg enzyme with 2',3'-cAMP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
Vmax=2.36 umol/min/mg enzyme with 2',3'-cGMP as substrate
{ECO:0000269|PubMed:15210699, ECO:0000269|PubMed:3516995};
pH dependence:
Optimum pH is 9.4 for AMP incorporation, 10.0 for CMP
incorporation, and 7.0 for the phosphatase and phosphodiesterase
activities. {ECO:0000269|PubMed:15210699,
ECO:0000269|PubMed:3516995};
-!- SUBUNIT: Monomer. Can also form homodimers and oligomers, but with
low levels. {ECO:0000269|PubMed:15210699}.
-!- INTERACTION:
P0A6M4:dtd; NbExp=2; IntAct=EBI-545256, EBI-562575;
-!- DOMAIN: Comprises two domains: an N-terminal domain containing the
nucleotidyltransferase activity and a C-terminal HD domain
associated with both phosphodiesterase and phosphatase activities.
-!- MISCELLANEOUS: A single active site specifically recognizes both
ATP and CTP and is responsible for their addition. {ECO:0000250}.
-!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M12788; AAA23541.1; -; Genomic_DNA.
EMBL; U28379; AAA89136.1; -; Genomic_DNA.
EMBL; U00096; AAC76092.1; -; Genomic_DNA.
EMBL; AP009048; BAE77107.1; -; Genomic_DNA.
PIR; A25215; RNECTA.
RefSeq; NP_417528.1; NC_000913.3.
RefSeq; WP_000708487.1; NZ_LN832404.1.
ProteinModelPortal; P06961; -.
SMR; P06961; -.
BioGrid; 4259255; 71.
DIP; DIP-9250N; -.
IntAct; P06961; 25.
STRING; 316385.ECDH10B_3231; -.
ChEMBL; CHEMBL3309020; -.
PaxDb; P06961; -.
PRIDE; P06961; -.
EnsemblBacteria; AAC76092; AAC76092; b3056.
EnsemblBacteria; BAE77107; BAE77107; BAE77107.
GeneID; 947553; -.
KEGG; ecj:JW3028; -.
KEGG; eco:b3056; -.
PATRIC; fig|1411691.4.peg.3675; -.
EchoBASE; EB0134; -.
EcoGene; EG10136; cca.
eggNOG; ENOG4105D4J; Bacteria.
eggNOG; COG0617; LUCA.
HOGENOM; HOG000007368; -.
InParanoid; P06961; -.
KO; K00974; -.
OMA; GWTFHGH; -.
PhylomeDB; P06961; -.
BioCyc; EcoCyc:EG10136-MONOMER; -.
BioCyc; MetaCyc:EG10136-MONOMER; -.
BRENDA; 2.7.7.72; 2026.
BRENDA; 3.1.4.16; 2026.
BRENDA; 3.1.4.37; 2026.
SABIO-RK; P06961; -.
PRO; PR:P06961; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0004810; F:tRNA adenylyltransferase activity; IDA:EcoCyc.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0016437; F:tRNA cytidylyltransferase activity; IDA:EcoCyc.
GO; GO:0042245; P:RNA repair; IMP:EcoCyc.
GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:EcoCyc.
CDD; cd00077; HDc; 1.
CDD; cd05398; NT_ClassII-CCAase; 1.
HAMAP; MF_01261; CCA_bact_type1; 1.
HAMAP; MF_01262; CCA_bact_type2; 1.
InterPro; IPR012006; CCA_bact.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR002646; PolA_pol_head_dom.
InterPro; IPR032828; PolyA_RNA-bd.
Pfam; PF01966; HD; 1.
Pfam; PF01743; PolyA_pol; 1.
Pfam; PF12627; PolyA_pol_RNAbd; 1.
PIRSF; PIRSF000813; CCA_bact; 1.
PROSITE; PS51831; HD; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Multifunctional enzyme; Nickel; Nucleotide-binding;
Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
Transferase; tRNA processing.
CHAIN 1 412 Multifunctional CCA protein.
/FTId=PRO_0000138975.
DOMAIN 228 329 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
METAL 21 21 Magnesium. {ECO:0000250}.
METAL 23 23 Magnesium. {ECO:0000250}.
BINDING 8 8 ATP or CTP; via amide nitrogen.
{ECO:0000250}.
BINDING 11 11 ATP or CTP. {ECO:0000250}.
BINDING 91 91 ATP or CTP. {ECO:0000250}.
BINDING 137 137 ATP or CTP. {ECO:0000250}.
BINDING 140 140 ATP or CTP. {ECO:0000250}.
MUTAGEN 21 21 D->A: No effect on phosphodiesterase and
phosphatase activities.
{ECO:0000269|PubMed:15210699}.
MUTAGEN 23 23 D->A: No effect on phosphodiesterase and
phosphatase activities.
{ECO:0000269|PubMed:15210699}.
MUTAGEN 70 70 G->D: Lowered AMP incorporation.
{ECO:0000269|PubMed:3533927}.
MUTAGEN 255 255 H->A: Loss of phosphodiesterase and
phosphatase activities.
{ECO:0000269|PubMed:15210699}.
MUTAGEN 256 256 D->A: Loss of phosphodiesterase and
phosphatase activities.
{ECO:0000269|PubMed:15210699}.
MUTAGEN 305 305 H->A: Loss of phosphodiesterase and
phosphatase activities.
{ECO:0000269|PubMed:15210699}.
MUTAGEN 306 306 D->A: Still possesses phosphodiesterase
and phosphatase activities.
{ECO:0000269|PubMed:15210699}.
SEQUENCE 412 AA; 46467 MW; 947182E6086220F7 CRC64;
MKIYLVGGAV RDALLGLPVK DRDWVVVGST PQEMLDAGYQ QVGRDFPVFL HPQTHEEYAL
ARTERKSGSG YTGFTCYAAP DVTLEDDLKR RDLTINALAQ DDNGEIIDPY NGLGDLQNRL
LRHVSPAFGE DPLRVLRVAR FAARYAHLGF RIADETLALM REMTHAGELE HLTPERVWKE
TESALTTRNP QVFFQVLRDC GALRVLFPEI DALFGVPAPA KWHPEIDTGI HTLMTLSMAA
MLSPQVDVRF ATLCHDLGKG LTPPELWPRH HGHGPAGVKL VEQLCQRLRV PNEIRDLARL
VAEFHDLIHT FPMLNPKTIV KLFDSIDAWR KPQRVEQLAL TSEADVRGRT GFESADYPQG
RWLREAWEVA QSVPTKAVVE AGFKGVEIRE ELTRRRIAAV ASWKEQRCPK PE


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