RPOA_HELPJ
ID RPOA_HELPJ Reviewed; 344 AA.
AC Q9ZJT5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha {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 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=jhp_1213;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06815.1; -; Genomic_DNA.
DR PIR; E71832; E71832.
DR RefSeq; WP_000864517.1; NZ_CP011330.1.
DR PDB; 2MAX; NMR; -; A=231-344.
DR PDBsum; 2MAX; -.
DR AlphaFoldDB; Q9ZJT5; -.
DR BMRB; Q9ZJT5; -.
DR SMR; Q9ZJT5; -.
DR STRING; 85963.jhp_1213; -.
DR EnsemblBacteria; AAD06815; AAD06815; jhp_1213.
DR GeneID; 66522487; -.
DR KEGG; hpj:jhp_1213; -.
DR PATRIC; fig|85963.30.peg.1358; -.
DR eggNOG; COG0202; Bacteria.
DR OMA; LMKFRNF; -.
DR Proteomes; UP000000804; Chromosome.
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..344
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175317"
FT REGION 1..238
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 254..344
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2MAX"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:2MAX"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:2MAX"
SQ SEQUENCE 344 AA; 38480 MW; 1F13FFA7EAE72F6C CRC64;
MKVIKTAPLI PSEIKVLEKE GNRVKISLAP FEFGYAVTLA HPIRRLLLLS SVGYAPVGLK
IEGVHHEFDS LRGVTEDVSL FIMNLKNIRF IAKALVGQDS SLENQSVVVD YSFKGPMELR
ARDLNSDHIE IVNPEMPLAT INEDAQLNFS LIIYKGMGYV PSENTRELMP EGYMPLDGSF
TPIKNVVYEI ENVLVEGDPN YEKIIFDIET DGQIDPYKAF LSAVKVMSKQ LGVFGERPIA
NTEYSGDYAQ RDDAKDLSAK IESMNLSARC FNCLDKIGIK YVGELVLMSE EELKGVKNMG
KKSYDEIAEK LNDLGYPVGT ELSPEQRESL KKRLEKLEDK GGND
