RPOC_RHORT
ID RPOC_RHORT Reviewed; 1393 AA.
AC Q2RQV4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Rru_A2694;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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_01322}.
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_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; CP000230; ABC23491.1; -; Genomic_DNA.
DR RefSeq; WP_011390504.1; NC_007643.1.
DR RefSeq; YP_427778.1; NC_007643.1.
DR AlphaFoldDB; Q2RQV4; -.
DR SMR; Q2RQV4; -.
DR STRING; 269796.Rru_A2694; -.
DR PRIDE; Q2RQV4; -.
DR EnsemblBacteria; ABC23491; ABC23491; Rru_A2694.
DR KEGG; rru:Rru_A2694; -.
DR PATRIC; fig|269796.9.peg.2802; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR PhylomeDB; Q2RQV4; -.
DR Proteomes; UP000001929; Chromosome.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1393
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240820"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1393 AA; 155038 MW; 261FC4C78C89EC21 CRC64;
MNELMKIFGQ VSGTQAFDQI KISIASPEKI RSWSFGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKY RGIICEKCGV EVTLSKVRRE RMGHIELAAP VAHIWFMKSL
PSRVGLLIDM TLKDLERVLY FENYVVVEPG LTPLKLHEML SEEQYQRAVE EYGEDSFTAG
IGAEAIRDML MSIDLETLKT DMKVELRDTT SEAKRKKLVK RLKIVDAFIE SGCRPEWMIL
EVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIIRNEKRML
QESVDALFDN GRRGRAITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELKLHQCGLP KKMALELFKP FVYSKLEQYH YATTIKAAKR MVEKERPEVW DILEEVIREH
PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCTAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPANGKPI IVPTQDIVLG LYYLTLDREG EKGEGMAFAS LNEIEHALQA
RVVSLQARVK ARLHTIDENG APVIRTVETT PGRMLLSRLL PRHTALPFSV INRLLRKKDI
TDVIDTVYRH CGQKETVIFC DRVMQLGYAH AARAGISFGK DDLVIPPTKA QLVADTDAEV
KEFEQQYQDG LITQGEKYNK VVDAWSHCTE RVADEMMKEI AKIEPGKPVN SVYMMAHSGA
RGSAAQMKQL AGMRGLMAKP SGEIIETPIV SNFKEGLTVL EYFNSTHGAR KGLADTALKT
ANSGYLTRRL VDVAQDAIIV IEDCGTSRGI TAMPVVEGGQ IIASLGERVL GRTAAEDIKD
TDGTIIVPLG KMIEEHDVEL LEEAGIEQVR IRSVLTCEAE TGICGKCYGR DLARGTKVNI
GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA QRGAEQSSVE AAFDGKIVME NRAVVGTSEN
VLIVMSRNCE VKITDEAGRE KARYRIPYGS KLLTDEGRMV TKGDRLAEWD PYTVPIITER
EGIAIYNDLV EGVSVREVTD EATGISSKVV VEWKNMPKGT DLKPRITLRD DRGEGITLAN
GLEARYFMSV DTILSVENGQ RVKAGDVLGR IPREGSKTRD ITGGLPRVAE LFEARKPKDH
AIISEIDGRV EFGKDYKSKR RLLVVPEDGD PVEYLLPKGK HLTIQEGDYV RKGDPLMDGN
PVPHDILRVM GVEALANYLI KEIQDVYRLQ GVKINDKHIE VISRQMLQKV EITEPGDTTF
LVGELIDRTD FQIENEKTLK ENGRPANSIP VLQGITKASL QTHSFISAAS FQETTRVLTE
AAVSGKSDSL MGLKENVIVG RLIPAGTGAM MNRLRALAAT RDKEIEDSRG AEMVPVLGAA
ESFTPRLPEP PAE
