ID   RPOC_TREDE              Reviewed;        1424 AA.
AC   Q73JJ8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=TDE_2420;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12938.1; -; Genomic_DNA.
DR   RefSeq; NP_973019.1; NC_002967.9.
DR   RefSeq; WP_002680359.1; NC_002967.9.
DR   AlphaFoldDB; Q73JJ8; -.
DR   SMR; Q73JJ8; -.
DR   STRING; 243275.TDE_2420; -.
DR   PRIDE; Q73JJ8; -.
DR   EnsemblBacteria; AAS12938; AAS12938; TDE_2420.
DR   GeneID; 2739845; -.
DR   KEGG; tde:TDE_2420; -.
DR   PATRIC; fig|243275.7.peg.2287; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_12; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000008212; 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; -; 2.
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..1424
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067822"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         783
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         857
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         864
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         867
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1424 AA;  160037 MW;  BC2778C13F3E30BC CRC64;
     MRDIQDFDSL MIRLASPDTI RAWSYGEVKK PETINYRTLR PERDGLFCER IFGTTKEWEC
     FCGKFKSIRY KGVICDRCGV EVTHFKVRRE RMGHIELAAP VSHIWYYRSV PSRMGLLLNL
     QVAALRSVLY YEKYIVIDAN DTDLEPMQLL TEDEYRDAHE RYGAAFTAGM GAGAIKTLLQ
     NINLDELAAQ LRAKMIEKGA KSDQRLLRRI EIVENFRASG NKPEWMILDV IPVIPPDLRP
     MVQLDGGRFA TSDLNDLYRR VIHRNSRLSK LMELKAPDII IRNEKRMLQE AVDALFDNSK
     RKKAIKGASN RPLKSISDLL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLWQCGLPTK
     MALELFKPFI MKKLVQKEVV SNIKKAKLLV EQEAAEVFAV LDEVVSEHPV LLNRAPTLHR
     LGIQAFEPVL VEGKAIRLHP LVCKAFNADF DGDQMAIHVP LTQAAQMECW TLMLSARNLL
     DPANGKTIVF PTQDMVLGLY YLTKERALPE GKKERLYSSV PEVLMAAECH AVGWQEPVLI
     DYETEPGKIE TVRTTPGRIL FNEEMPEGVP FTNYALNDKK IRKLIENVFK DKGPWLAVQL
     LDKLKAVGYK YATYFGATLS MEDMIIPPEK AGMLEKANKE VLEIYNQYKG GHITQEERYN
     RVVDVWQKTN SNLKEILMKR LQEDKGGFNT IHMMETSGAR GSKDQINQLA GMRGLMSKPT
     GDIIELPIRS NFKEGLNVME FFISTNGARK GLTDTALKTS DAGYLTRRLV DIAQNVVVNE
     EDCGTINGIE YAAIKRGDEI RESLSERIAG KYTLERVIHP ITGELLIDVN EYITDETAKK
     IEEAGVETVK LRTVLTCESK HGVCVKCYGR DLARNRIVRI GEAVGIIAAQ SIGQPGTQLT
     MRTFHEGGTA SKNVEENRIV FNDYSIIVRG IKGSYVTLKN GHFLFTRKGE FTFSRVLNEY
     ALKKGETALV STGTRVVKGN PLYTLKNGKE VLSENIAIAE VRDNIIYLTG QEQTIEIRNG
     SEVVVKENDV IKAGETVGTF DPFADPILAE YDGFVRFEDI LPGTTLKEEA DEETGVVEKR
     ISDAHFDKMQ PRIFISDESG NTVGEDSYFL PGGAQLLVEE GQEIKAGAIL AKIAKESVKT
     KDITGGLPRV SELLEARRPK SPAVLAAIAG VVTIKKGLLK GKRTIMVRDE YGHDVKHLVP
     IGKRMLVRDG DTVKAGEPLC DGSFDPHDIL NILGENALQN YLMKEIKEVY DAQGVTINDK
     HVGIIVRQML RKVKIVSVGD TKFIFDQQID KYRFHEENKR VKEEGGQPAV ARPMFQGITK
     AALNIDSFIS AASFQETTKV LTNAAIAGSS DELRGLKENV IIGHLIPAGT GMKQYRDIKL
     FDKNKSDLDI QMNEILERRR LEAEAAQALE EKELIEEENF LDDL