ID   PCNB_ECO57              Reviewed;         465 AA.
AC   P0ABF3; P13685; P78050; Q8X910;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 97.
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};
GN   Name=pcnB {ECO:0000255|HAMAP-Rule:MF_00957};
GN   OrderedLocusNames=Z0154, ECs0147;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00957}.
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};
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000255|HAMAP-Rule:MF_00957}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB33570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG54447.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33570.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_308174.3; NC_002695.1.
DR   RefSeq; WP_010723084.1; NZ_VOAI01000002.1.
DR   AlphaFoldDB; P0ABF3; -.
DR   SMR; P0ABF3; -.
DR   STRING; 155864.Z0154; -.
DR   GeneID; 75170043; -.
DR   GeneID; 913763; -.
DR   KEGG; ece:Z0154; -.
DR   KEGG; ecs:ECs_0147; -.
DR   PATRIC; fig|386585.9.peg.246; -.
DR   eggNOG; COG0617; Bacteria.
DR   HOGENOM; CLU_015961_0_0_6; -.
DR   OMA; FMAKLDM; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043633; P:polyadenylation-dependent RNA catabolic process; IEA:InterPro.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 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   NCBIfam; TIGR01942; pcnB; 1.
DR   PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12626; PolyA_pol_arg_C; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Reference proteome;
KW   RNA-binding; Transcription; Transferase.
FT   CHAIN           1..465
FT                   /note="Poly(A) polymerase I"
FT                   /id="PRO_0000139091"
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"
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
//