RPOA_XANOP
ID RPOA_XANOP Reviewed; 332 AA.
AC B2SQT4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=PXO_04496;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(2008).
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; CP000967; ACD57911.1; -; Genomic_DNA.
DR RefSeq; WP_002811635.1; NC_010717.2.
DR PDB; 6J9E; EM; 3.41 A; A/B=1-332.
DR PDB; 6J9F; EM; 3.95 A; A/B=1-332.
DR PDBsum; 6J9E; -.
DR PDBsum; 6J9F; -.
DR AlphaFoldDB; B2SQT4; -.
DR SMR; B2SQT4; -.
DR STRING; 360094.PXO_04496; -.
DR EnsemblBacteria; ACD57911; ACD57911; PXO_04496.
DR GeneID; 61895222; -.
DR GeneID; 64095479; -.
DR GeneID; 67405829; -.
DR KEGG; xop:PXO_04496; -.
DR eggNOG; COG0202; Bacteria.
DR HOGENOM; CLU_053084_0_1_6; -.
DR OMA; LMKFRNF; -.
DR OrthoDB; 662686at2; -.
DR Proteomes; UP000001740; 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..332
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_1000091975"
FT REGION 1..234
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 248..332
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 21..31
FT /evidence="ECO:0007829|PDB:6J9E"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6J9E"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6J9E"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:6J9E"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6J9E"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:6J9E"
SQ SEQUENCE 332 AA; 36364 MW; 3F8A9945966DFFB9 CRC64;
MTVTANQVLR PRGPQIERLT DNRAKVVIEP LERGYGHTLG NALRRVLLSS IPGFAITEVE
IDGVLHEYTT VEGLQEDVLD VLLNLKDVAI RMHSGDSATL SLSKQGPGTV TAADIRTDHN
VEIINGDHVI CHLTKDTALN MRLKIERGFG YQPAAARRRP DEETRTIGRL MLDASFSPVR
RVAYAVEAAR VEQRTDLDKL VIDIETNGTI DAEEAVRTAA DILSDQLSVF GDFTHRDRGA
AKPAASGVDP VLLRPIDDLE LTVRSANCLK AESIYYIGDL IQKTEVELLK TPNLGKKSLT
EIKEVLAQRG LALGMKLENW PPAGVAQHGM LG
