RPOA_CAMJE
ID RPOA_CAMJE Reviewed; 337 AA.
AC Q9PM80; Q0P833;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=Cj1595;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35692.1; -; Genomic_DNA.
DR PIR; A81255; A81255.
DR RefSeq; WP_002851403.1; NC_002163.1.
DR RefSeq; YP_002344964.1; NC_002163.1.
DR PDB; 4NOI; X-ray; 2.17 A; A/B=1-337.
DR PDBsum; 4NOI; -.
DR AlphaFoldDB; Q9PM80; -.
DR SMR; Q9PM80; -.
DR IntAct; Q9PM80; 2.
DR STRING; 192222.Cj1595; -.
DR PaxDb; Q9PM80; -.
DR PRIDE; Q9PM80; -.
DR EnsemblBacteria; CAL35692; CAL35692; Cj1595.
DR GeneID; 905865; -.
DR KEGG; cje:Cj1595; -.
DR PATRIC; fig|192222.6.peg.1571; -.
DR eggNOG; COG0202; Bacteria.
DR HOGENOM; CLU_053084_0_1_7; -.
DR OMA; LMKFRNF; -.
DR Proteomes; UP000000799; 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 Reference proteome; Transcription; Transferase.
FT CHAIN 1..337
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175284"
FT REGION 1..231
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 247..337
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT STRAND 13..32
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 97..112
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 175..188
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 191..203
FT /evidence="ECO:0007829|PDB:4NOI"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:4NOI"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4NOI"
SQ SEQUENCE 337 AA; 37686 MW; 4BD2F59205DDE143 CRC64;
MRNITTSAYT PTEFTIENIS DTVAKISAWP FEIGYGITLA HPLRRLLYTS TIGYAPTAIH
IDGVAHEFDS MRGMLEDVAL FIINLKKLRF KIKGDSNKEI VEFSFKGSKE IYGKDLNNDQ
VEVVNKDAYL ATINEDAELK FTLIVEKGIG YVPSEEIKEL INDPKFIALD AFFTPVREAT
YDIEKVLFED NPDYEKVVLT VTTDGQITPN EAFQNALEAM YKQLSVFDKI TNVRSVIKNQ
ATSNELENTK LLQNITDLNL SARSYNCLEK AGVVYIGELA LMSVSELAGL KNLGKKSLDE
IKNIMESIGF PVGTSKLSDN KEILKNKIAE LKAQNEG
