RPOA1_FRATH
ID RPOA1_FRATH Reviewed; 323 AA.
AC Q2A5E5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=FTL_0261;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM233362; CAJ78702.1; -; Genomic_DNA.
DR RefSeq; WP_003021582.1; NZ_CP009694.1.
DR PDB; 6WMP; EM; 2.98 A; A=1-323.
DR PDB; 6WMR; EM; 3.46 A; A=1-323.
DR PDB; 6WMT; EM; 4.43 A; A=1-323.
DR PDBsum; 6WMP; -.
DR PDBsum; 6WMR; -.
DR PDBsum; 6WMT; -.
DR AlphaFoldDB; Q2A5E5; -.
DR SMR; Q2A5E5; -.
DR KEGG; ftl:FTL_0261; -.
DR OMA; LMKFRNF; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR011262; DNA-dir_RNA_pol_insert.
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; PF01000; RNA_pol_A_bac; 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..323
FT /note="DNA-directed RNA polymerase subunit alpha 1"
FT /id="PRO_0000296802"
FT REGION 1..228
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 244..323
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:6WMP"
SQ SEQUENCE 323 AA; 35358 MW; D9F934544A63E27F CRC64;
MSNNNSKLEF VPNIQLKEDL GAFSYKVQLS PVEKGMAHIL GNSIRRVLLS SLSGASIIKV
NIANVLHEYS TLEDVKEDVV EIVSNLKKVA IKLDTGIDRL DLELSVNKSG VVSAGDFKTT
QGVEIINKDQ PIATLTNQRA FSLTATVSVG RNVGILSAIP TELERVGDIA VDADFNPIKR
VAFEVFDNGD SETLEVFVKT NGTIEPLAAV TKALEYFCEQ ISVFVSLRVP SNGKTGDVLI
DSNIDPILLK PIDDLELTVR SSNCLRAENI KYLGDLVQYS ESQLMKIPNL GKKSLNEIKQ
ILIDNNLSLG VQIDNFRELV EGK
