RPOA2_FRATH
ID RPOA2_FRATH Reviewed; 317 AA.
AC Q2A4H7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=FTL_0616;
OS Francisella tularensis subsp. holarctica (strain LVS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=376619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVS;
RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA Garcia E.;
RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT Strain).";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AM233362; CAJ79056.1; -; Genomic_DNA.
DR RefSeq; WP_003015012.1; NZ_CP009694.1.
DR PDB; 6WMP; EM; 2.98 A; B=1-317.
DR PDB; 6WMR; EM; 3.46 A; B=1-317.
DR PDB; 6WMT; EM; 4.43 A; B=1-317.
DR PDBsum; 6WMP; -.
DR PDBsum; 6WMR; -.
DR PDBsum; 6WMT; -.
DR AlphaFoldDB; Q2A4H7; -.
DR SMR; Q2A4H7; -.
DR KEGG; ftl:FTL_0616; -.
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.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Transcription; Transferase.
FT CHAIN 1..317
FT /note="DNA-directed RNA polymerase subunit alpha 2"
FT /id="PRO_0000296803"
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"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6WMP"
SQ SEQUENCE 317 AA; 35074 MW; 6F740ECAAFA38F21 CRC64;
MALENLLHPT NIKIDEYAKN ATKFSFEALE RGVGYTLGFA LKQTMLYSIA GACVTSIKIN
DGKVTSLEDV IPCDETVADI ILNVKSLSVT LAEDVETGTI TFELSGSEEE IFSEEAKLSE
GLAITEEVFI CSYNGGKKLK IEAKVEKGVG FRPAQDNFKD GEFLLDATFS PVVFCDFEIK
DARVGRRTDL DKLELNIKTN GNVNCEEALR LAATKIQNQL RNIVDIEEIN KGIFVEDPKD
INPILLKHVE ELNLTARSSN CLKAVNIRLI GELVQKTENE LLKAPNFGKK SLTEIKDKLS
ELGLSLGTLI ENWPQDL
