RPOA2_FRATF
ID RPOA2_FRATF Reviewed; 317 AA.
AC A7NAX2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=RNA polymerase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=FTA_0649;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00059};
CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription. {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators and with upstream promoter elements.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR EMBL; CP000803; ABU61125.1; -; Genomic_DNA.
DR RefSeq; WP_010031988.1; NC_009749.1.
DR AlphaFoldDB; A7NAX2; -.
DR SMR; A7NAX2; -.
DR KEGG; fta:FTA_0649; -.
DR HOGENOM; CLU_053084_0_0_6; -.
DR OMA; MFIYETR; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR011260; RNAP_asu_C.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
DR Pfam; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..317
FT /note="DNA-directed RNA polymerase subunit alpha 2"
FT /id="PRO_0000323635"
FT REGION 1..227
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 241..317
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ SEQUENCE 317 AA; 35120 MW; 05B40866C78FA5A1 CRC64;
MALENLLHPT NIKIDEYAKN ATKFSFEALE RGVGYTLGFA LKQTMLYSIA GACVTSIKIN
DGKVTSLEDV IPCDETVADI ILNVKSLSVT LAEDVETGTI TFELSGSEEE IFSEEAKLSE
GLAITEEVFI CSYNGGKKLK IEAKVEKGVG FRPAQDNFKD CEFLLDATFS PVVFCDFEIK
DARVGRRTDL DKLELNIKTN GNVNCEEALR LAATKIQNQL RNIVDIEEIN KGIFVEDPKD
INPILLKHVE ELNLTARSSN CLKAVNIRLI GELVQKTENE LLKAPNFGKK SLTEIKDKLS
ELGLSLGTLI ENWPQDL