PCNB_ECOLI
ID PCNB_ECOLI Reviewed; 465 AA.
AC P0ABF1; P13685; P78050; Q8X910;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Poly(A) polymerase I {ECO:0000255|HAMAP-Rule:MF_00957};
DE Short=PAP I {ECO:0000255|HAMAP-Rule:MF_00957};
DE EC=2.7.7.19 {ECO:0000255|HAMAP-Rule:MF_00957};
DE AltName: Full=Plasmid copy number protein;
DE Flags: Precursor;
GN Name=pcnB {ECO:0000255|HAMAP-Rule:MF_00957};
GN OrderedLocusNames=b0143, JW5808;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / RP437;
RX PubMed=2537812; DOI=10.1128/jb.171.3.1254-1261.1989;
RA Liu J., Parkinson J.S.;
RT "Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene
RT involved in plasmid copy number control.";
RL J. Bacteriol. 171:1254-1261(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, PROTEIN SEQUENCE OF 11-25,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=1438224; DOI=10.1073/pnas.89.21.10380;
RA Cao G.-J., Sarkar N.;
RT "Identification of the gene for an Escherichia coli poly(A) polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10380-10384(1992).
RN [6]
RP SIMILARITY TO CCA.
RX PubMed=1691435; DOI=10.1007/bf00260507;
RA Masters M., March J.B., Oliver I.R., Collins J.F.;
RT "A possible role for the pcnB gene product of Escherichia coli in
RT modulating RNA: RNA interactions.";
RL Mol. Gen. Genet. 220:341-344(1990).
RN [7]
RP MUTAGENESIS, AND INTERACTION WITH CSDA; RHLE AND SRMB.
RX PubMed=10361280; DOI=10.1046/j.1365-2958.1999.01394.x;
RA Raynal L.C., Carpousis A.J.;
RT "Poly(A) polymerase I of Escherichia coli: characterization of the
RT catalytic domain, an RNA binding site and regions for the interaction with
RT proteins involved in mRNA degradation.";
RL Mol. Microbiol. 32:765-775(1999).
RN [8]
RP FUNCTION.
RC STRAIN=MG1693;
RX PubMed=10594833; DOI=10.1046/j.1365-2958.1999.01673.x;
RA Mohanty B.K., Kushner S.R.;
RT "Analysis of the function of Escherichia coli poly(A) polymerase I in RNA
RT metabolism.";
RL Mol. Microbiol. 34:1094-1108(1999).
RN [9]
RP IDENTIFICATION OF INITIATION SITE.
RX PubMed=12068810; DOI=10.1046/j.1365-2958.2002.02945.x;
RA Binns N., Masters M.;
RT "Expression of the Escherichia coli pcnB gene is translationally limited
RT using an inefficient start codon: a second chromosomal example of
RT translation initiated at AUU.";
RL Mol. Microbiol. 44:1287-1298(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15737627; DOI=10.1016/j.bbrc.2005.02.025;
RA Jasiecki J., Wegrzyn G.;
RT "Localization of Escherichia coli poly(A) polymerase I in cellular
RT membrane.";
RL Biochem. Biophys. Res. Commun. 329:598-602(2005).
RN [11]
RP FUNCTION.
RC STRAIN=MG1693;
RX PubMed=17040898; DOI=10.1093/nar/gkl684;
RA Mohanty B.K., Kushner S.R.;
RT "The majority of Escherichia coli mRNAs undergo post-transcriptional
RT modification in exponentially growing cells.";
RL Nucleic Acids Res. 34:5695-5704(2006).
RN [12]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20700605; DOI=10.1007/s00438-010-0567-y;
RA Nadratowska-Wesolowska B., Slominska-Wojewodzka M., Lyzen R., Wegrzyn A.,
RA Szalewska-Palasz A., Wegrzyn G.;
RT "Transcription regulation of the Escherichia coli pcnB gene coding for
RT poly(A) polymerase I: roles of ppGpp, DksA and sigma factors.";
RL Mol. Genet. Genomics 284:289-305(2010).
CC -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which usually
CC targets these RNAs for decay. Plays a significant role in the global
CC control of gene expression, through influencing the rate of transcript
CC degradation, and in the general RNA quality control. Rho-independent
CC transcription terminators may serve as polyadenylation signals. Seems
CC to be involved in plasmid copy number control. {ECO:0000255|HAMAP-
CC Rule:MF_00957, ECO:0000269|PubMed:10594833, ECO:0000269|PubMed:1438224,
CC ECO:0000269|PubMed:17040898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00957, ECO:0000269|PubMed:1438224};
CC -!- SUBUNIT: Monomer. Interacts with CsdA, RhlE and SrmB.
CC {ECO:0000269|PubMed:10361280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15737627}. Cell
CC inner membrane {ECO:0000269|PubMed:15737627}.
CC -!- INDUCTION: Transcription regulation of pcnB is a complex process that
CC involves several factors such as Sigma-70 (rpoD), Sigma-S (rpoS), ppGpp
CC and DksA. {ECO:0000269|PubMed:20700605}.
CC -!- MISCELLANEOUS: Uses the non-canonical initiation codon AUU, which
CC limits pcnB expression. {ECO:0000305|PubMed:12068810}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000255|HAMAP-Rule:MF_00957}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24303.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB24139.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M20574; AAA24303.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73254.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96720.2; -; Genomic_DNA.
DR EMBL; S48039; AAB24139.1; ALT_INIT; Genomic_DNA.
DR PIR; G64737; G64737.
DR RefSeq; NP_414685.4; NC_000913.3.
DR RefSeq; WP_010723084.1; NZ_CP014272.1.
DR AlphaFoldDB; P0ABF1; -.
DR SMR; P0ABF1; -.
DR BioGRID; 4263029; 32.
DR DIP; DIP-47859N; -.
DR IntAct; P0ABF1; 12.
DR STRING; 511145.b0143; -.
DR jPOST; P0ABF1; -.
DR PaxDb; P0ABF1; -.
DR PRIDE; P0ABF1; -.
DR EnsemblBacteria; AAC73254; AAC73254; b0143.
DR EnsemblBacteria; BAB96720; BAB96720; BAB96720.
DR GeneID; 58461933; -.
DR GeneID; 947318; -.
DR KEGG; ecj:JW5808; -.
DR KEGG; eco:b0143; -.
DR PATRIC; fig|511145.12.peg.148; -.
DR EchoBASE; EB0684; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_0_6; -.
DR InParanoid; P0ABF1; -.
DR OMA; FMAKLDM; -.
DR PhylomeDB; P0ABF1; -.
DR BioCyc; EcoCyc:EG10690-MON; -.
DR BioCyc; MetaCyc:EG10690-MON; -.
DR BRENDA; 2.7.7.19; 2026.
DR PRO; PR:P0ABF1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0003723; F:RNA binding; IMP:EcoliWiki.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:EcoliWiki.
DR GO; GO:0006397; P:mRNA processing; IDA:EcoliWiki.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoliWiki.
DR GO; GO:0009451; P:RNA modification; IDA:EcoliWiki.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_00957; PolyA_pol; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR010206; PolA_pol_I.
DR InterPro; IPR025866; PolyA_pol_arg_C_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12626; PolyA_pol_arg_C; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01942; pcnB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; mRNA processing; Nucleotide-binding;
KW Plasmid copy control; Reference proteome; RNA-binding; Transcription;
KW Transferase.
FT PROPEP 1..10
FT /evidence="ECO:0000269|PubMed:1438224"
FT /id="PRO_0000411163"
FT CHAIN 11..465
FT /note="Poly(A) polymerase I"
FT /id="PRO_0000139090"
FT REGION 429..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
FT ACT_SITE 82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
FT CONFLICT 93
FT /note="R -> A (in Ref. 1; AAA24303)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="A -> T (in Ref. 1; AAA24303)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="K -> N (in Ref. 1; AAA24303)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..438
FT /note="ML -> IV (in Ref. 1; AAA24303)"
FT /evidence="ECO:0000305"
FT CONFLICT 449..465
FT /note="RRTRRPRKRAPRREGTA -> QSYSSSTQTRTTS (in Ref. 1;
FT AAA24303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53871 MW; 0FAE30F2F95FB76E CRC64;
MFTRVANFCR KVLSREESEA EQAVARPQVT VIPREQHAIS RKDISENALK VMYRLNKAGY
EAWLVGGGVR DLLLGKKPKD FDVTTNATPE QVRKLFRNCR LVGRRFRLAH VMFGPEIIEV
ATFRGHHEGN VSDRTTSQRG QNGMLLRDNI FGSIEEDAQR RDFTINSLYY SVADFTVRDY
VGGMKDLKDG VIRLIGNPET RYREDPVRML RAVRFAAKLG MRISPETAEP IPRLATLLND
IPPARLFEES LKLLQAGYGY ETYKLLCEYH LFQPLFPTIT RYFTENGDSP MERIIEQVLK
NTDTRIHNDM RVNPAFLFAA MFWYPLLETA QKIAQESGLT YHDAFALAMN DVLDEACRSL
AIPKRLTTLT RDIWQLQLRM SRRQGKRAWK LLEHPKFRAA YDLLALRAEV ERNAELQRLV
KWWGEFQVSA PPDQKGMLNE LDEEPSPRRR TRRPRKRAPR REGTA
