ID   RPOC_PETMO              Reviewed;        1643 AA.
AC   A9BF32;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Pmob_0354;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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_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}.
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; CP000879; ABX31096.1; -; Genomic_DNA.
DR   RefSeq; WP_012208203.1; NC_010003.1.
DR   AlphaFoldDB; A9BF32; -.
DR   SMR; A9BF32; -.
DR   STRING; 403833.Pmob_0354; -.
DR   PRIDE; A9BF32; -.
DR   EnsemblBacteria; ABX31096; ABX31096; Pmob_0354.
DR   KEGG; pmo:Pmob_0354; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000000789; 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; 2.
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.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1643
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353404"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         684
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         686
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         688
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1046
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1643 AA;  187027 MW;  831E86A6BA95E348 CRC64;
     MANVSSFQRK IAKIKIGIAS PQSILEASNG EVKKPETLNH RTGKPEKDGL FCEKIFGPVK
     DYECACGKYK GKKYEGTVCE RCGVKVESKE ARRRKIGHIE LATPISHIWY LKSSPSILSI
     ILNIGVKDLE NIIYYGSKRV IERAYLTLPG PENENLGYLP GEILYQREYE IYDEYLDLRV
     EPAVKIVSVK GMPVADIDGK VEIKSELTHT ERELNWIIIR DDTGVERKYP VFEGSSIMVE
     NGQEVEKGTP LADRFLFEED YLTQKEYSLF LEYYPGSIEV ERDIERDTPI VVITDIDKRF
     AKRIDKKIGD ILLEDEARAY EEVMKVLNSK IKEERENVID KELVSEIEFP EKKFEKGTKI
     TQEVLNELQE FGVKDLVAKE EDGTEKIFQI NRYEKFEYGY GAEAIQKLLT KIDLEVLKAR
     LESELEKLDR KSQKSVKILR RLKLVKDFIK SGNQPEWLIT NIIPVIPPDL RPLIQIDGGR
     FAATDLNDLY RKVINRNNRL RKLLEMEAPE IIVRNEKRIL QQAVDSLFYN GRVGKPMTDR
     NRRPLRSLTD LLKGKKGRFR RNLLGKRVDY SGRAVIAVGP DLKIHECGLP KKMALELFKP
     FVLAELLRDS NVASKSARKF KKTIIEKEMP EAWEVLEEVI KGHPVLLNRA PTLHRVSIQA
     FIPKLIEGNA IRLHPLVCPP FNADFDGDQM AIHIPLSNIA QAESKFLMLS RYNIISPANG
     KPLSMPGKDI IAGAYYLTMH EDEKFKNLKV PTKVSELGKN GYVKHIFSED LEATYAYEYL
     KIVDSDIYLQ DGKLIWKKSD LPLHEPVAFR YKDGSILKTT IGKIIFNEEV PEDLRDYTQK
     MDKKNLKELI FNTFEKHGID RTADLLDSIK DFGFHYATLS GLTISIRDVL VSPKREELIE
     ESKGEVLRIE SLYEEGYLTD NERYKEIIKI WESATAKVTE ETAKTYRKYT FNPIWMMIES
     GARGNIDQLK QLAGMRGLMA DPSGKIIEVP ITSNFKNGLS ELEFFTSTHG SRKGSADTAL
     RTSTAGYLTR RLVDVAQSIT ITEEDCGTDK GIEARELWAD DSKIENLSDF LFGRVLAKDV
     LDPETKEVIF NPQADKKYER GIILKEKDAQ FLANYVKEIP VSKEKTIKIE DMPKDSYLES
     LEDVQVEGKV LIKKGEEITE EAIEEAFLHG IQKLDVKEYT AVDYVYSGED LKVEIDGKTV
     TLLKYQERID LKVSKVLEKH GIKTVTVRPS IFIRSPLTCE SENGLCAKCY GMDLSNYKLV
     NRGEAVGIIA AQSIGEPGTQ LTMRTFHTGG IATTSDITQG LPRAEELFEA RKKTKGPEGE
     FSKTKGIVRA IERDTENKRG RRLKIIIENS DGELESYEAD YRTKAVVEEG DKVLAGQRLT
     TGNIKPRNIL KELGVGPLAN YLLSEIKKIY AEQGVDIHDK HFEIIIRQMI NKVEIIDGGD
     TDFMPGDLVS YGKVQKINEE ILEENSYITE NRELVVGKKL AKRVIIPAED EEEEEDKIFE
     QGTEITEEIL NQIIETNIKE IEVYEEYKEI TTEEGKTHLV GTSKKYLINP KDTIKYERRL
     LRITKASLER EGWLSAASFQ QTVQILTEAA IEGKVDRLKG LKENVIVGQP IPAGTGLKLY
     ADQNYEVVQP EKEAEAAQEK SVG