ID   CCA_ECOUT               Reviewed;         412 AA.
AC   Q1R6S5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Multifunctional CCA protein;
DE   Includes:
DE     RecName: Full=CCA-adding enzyme;
DE              EC=2.7.7.25;
DE              EC=2.7.7.21;
DE     AltName: Full=tRNA nucleotidyltransferase;
DE     AltName: Full=tRNA adenylyl-/cytidylyl-transferase;
DE     AltName: Full=tRNA CCA-pyrophosphorylase;
DE     AltName: Full=tRNA-NT;
DE   Includes:
DE     RecName: Full=2'-nucleotidase;
DE              EC=3.1.3.-;
DE   Includes:
DE     RecName: Full=2',3'-cyclic phosphodiesterase;
DE              EC=3.1.4.-;
DE   Includes:
DE     RecName: Full=Phosphatase;
DE              EC=3.1.3.-;
GN   Name=cca; OrderedLocusNames=UTI89_C3492;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid
CC       template. Adds these three nucleotides in the order of C, C, and A
CC       to the tRNA nucleotide-73, using CTP and ATP as substrates and
CC       producing inorganic pyrophosphate. Also shows phosphatase, 2'-
CC       nucleotidase and 2',3'-cyclic phosphodiesterase activities. These
CC       phosphohydrolase activities are probably involved in the repair of
CC       the tRNA 3'-CCA terminus degraded by intracellular RNases (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- COFACTOR: Magnesium for nucleotidyltransferase activity (By
CC       similarity).
CC   -!- COFACTOR: Nickel for phosphatase activity (By similarity).
CC   -!- SUBUNIT: Monomer. Can also form homodimers and oligomers (By
CC       similarity).
CC   -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC       nucleotidyltransferase activity and a C-terminal HD domain
CC       associated with both phosphodiesterase and phosphatase activities
CC       (By similarity).
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both
CC       ATP and CTP and is responsible for their addition (By similarity).
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
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DR   EMBL; CP000243; ABE08939.1; -; Genomic_DNA.
DR   RefSeq; YP_542470.1; -.
DR   GeneID; 3993898; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3492.
DR   KEGG; eci:UTI89_C3492; -.
DR   HOGENOM; Q1R6S5; -.
DR   OMA; Q1R6S5; KHHGHGQ.
DR   BioCyc; ECOL364106:UTI89_C3492-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:HAMAP.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:HAMAP.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:HAMAP.
DR   HAMAP; MF_01261; -; 1.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR003607; Met-dep_phosphohydro_HD.
DR   InterPro; IPR006674; Met-dep_phosphohydro_HD_sub.
DR   InterPro; IPR002646; PolyA_pol_reg.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
DR   SMART; SM00471; HDc; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nickel; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW   tRNA processing.
FT   CHAIN         1    412       Multifunctional CCA protein.
FT                                /FTId=PRO_1000054264.
FT   METAL        21     21       Magnesium (By similarity).
FT   METAL        23     23       Magnesium (By similarity).
FT   BINDING       8      8       ATP or CTP; via amide nitrogen (By
FT                                similarity).
FT   BINDING      11     11       ATP or CTP (By similarity).
FT   BINDING      91     91       ATP or CTP (By similarity).
FT   BINDING     137    137       ATP or CTP (By similarity).
FT   BINDING     140    140       ATP or CTP (By similarity).
SQ   SEQUENCE   412 AA;  46538 MW;  6AFE8DA5A89A6BB2 CRC64;
     MKIYLVGGAV RDALLGLPVK DRDWVVVGST PQEMLDAGYQ QVGRDFPVFL HPQTHEEYAL
     ARTERKSGSG YTGFTCYAAP DVTLEDDLKR RDLTINALAQ DDNGEIIDPY NGLGDLQNRL
     LRHVSPAFGE DPLRVLRVAR FAARYAHLCF RIADETLALM REMTHAGELE HLTPERVWKE
     TENALTTRNP QVFFQVLRDC GALRVLFPEI DALFGVPAPA RWHPEIDTGI HTLMTLSMAA
     MLSPQVDVRF ATLCHDLGKG LTPPELWPRH HGHGPAGVKL VEQLCQRLRV PNEIRDLARL
     VAEFHDLIHT FPMLNPKTIV KLFDSIDAWR KPQRVEQLAL TSEADVRGRT GFESADYPQG
     RWLREAWEVA QSVPTKAVVE AGFKGVEIRE ELTRRRIAAV AGWKEQRCPK PE
//