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CCA_ECOBW
ID   CCA_ECOBW               Reviewed;         412 AA.
AC   C4ZQX3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Multifunctional CCA protein {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=2'-nucleotidase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=Phosphatase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
GN   Name=cca {ECO:0000255|HAMAP-Rule:MF_01261}; OrderedLocusNames=BWG_2767;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid template.
CC       Adds these three nucleotides in the order of C, C, and A to the tRNA
CC       nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC       pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic
CC       phosphodiesterase activities. These phosphohydrolase activities are
CC       probably involved in the repair of the tRNA 3'-CCA terminus degraded by
CC       intracellular RNases. {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC         diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC         COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC       Note=Magnesium is required for nucleotidyltransferase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01261};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC       Note=Nickel for phosphatase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_01261};
CC   -!- SUBUNIT: Monomer. Can also form homodimers and oligomers.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC       nucleotidyltransferase activity and a C-terminal HD domain associated
CC       with both phosphodiesterase and phosphatase activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC       and CTP and is responsible for their addition. {ECO:0000255|HAMAP-
CC       Rule:MF_01261}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
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DR   EMBL; CP001396; ACR63259.1; -; Genomic_DNA.
DR   RefSeq; WP_000708487.1; NC_012759.1.
DR   AlphaFoldDB; C4ZQX3; -.
DR   SMR; C4ZQX3; -.
DR   KEGG; ebw:BWG_2767; -.
DR   HOGENOM; CLU_015961_1_1_6; -.
DR   OMA; GWTFHGH; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   HAMAP; MF_01261; CCA_bact_type1; 1.
DR   HAMAP; MF_01262; CCA_bact_type2; 1.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW   Nickel; Nucleotide-binding; Nucleotidyltransferase; RNA repair;
KW   RNA-binding; Transferase; tRNA processing.
FT   CHAIN           1..412
FT                   /note="Multifunctional CCA protein"
FT                   /id="PRO_1000214130"
FT   DOMAIN          228..329
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   BINDING         8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         8
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         11
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         91
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         137
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         140
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
SQ   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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