ID   RPOC_ENDTX              Reviewed;        1593 AA.
AC   B1GZ76;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=TGRD_075;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(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_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; AP009510; BAG13558.1; -; Genomic_DNA.
DR   RefSeq; WP_015423087.1; NC_020419.1.
DR   RefSeq; YP_001956019.1; NC_020419.1.
DR   AlphaFoldDB; B1GZ76; -.
DR   SMR; B1GZ76; -.
DR   STRING; 471821.TGRD_075; -.
DR   PRIDE; B1GZ76; -.
DR   EnsemblBacteria; BAG13558; BAG13558; TGRD_075.
DR   KEGG; rsd:TGRD_075; -.
DR   PATRIC; fig|471821.5.peg.118; -.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001691; 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.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1593
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353452"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         648
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         650
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         652
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1026
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1593 AA;  179214 MW;  B73D774EC40752B2 CRC64;
     MVKINFQIKK KKSNGPNFIG FDAVRVSVAS PDQIKTWSYG EVKKPETINY RTFKPERDGL
     FCNRIFGPTK DWECHCGKYK YIKYKGTICD RCGVEVTESK VRRERFGHIN LAVPVAHLWF
     LKKPPSRVGI LLNMKISDLE KVIYYAKYIV MGDLKDRSGI SFFARKGMLM GGEDFNLFKY
     GINNPIVKEE FKNIFDGIVC EEIKLDSNLT KALKQLKVLV KGQADSAGIS TEEAAKKILE
     NVKKGDIYYK VYFKPHSVYY YIDLDPSSHG EIKKILSEKF EKSSTVSITE TDKKIRIEFF
     DIEKDKIYND LRKDSFALKK YEGCLRIEIL KNKIPFIENF SRSDSFVLLE ESDINNIQNG
     FGDSLKVNIG AEAVRSLLEE INLDDEMKNI YAEIKKTKSD AERARLLRKL RVVEGFLNSQ
     TRPEWMILTV LPVIPPDLRP LVALDGGRFA TSDLNDLYRR IINRNNRLRH IEQLKAPIVM
     INNEKRLLQE AVDALIDNDS RMRPVTGAGN RILKSLSDTL KGKRGRFRQN LLGKRVDYSG
     RSVIVVGPNL RLNQCGIPKE MALELFKPFI VKELIKQENI TLRSAKRMLE RGDLKVWNIL
     EKVTQSHPVL LNRAPTLHRL GIQAFEPVLV EGKSIQLHPL TCSAFNADFD GDQMAVHLPI
     SLEAQLEARV LMMATRNILS PASGRPIAVP SQDMVLGNCY LTKEKYGVVG EGKVFSSVSE
     AISAYQAEKV DLQARIKVAG ITSIRDKNLN NDDEQPDVTK WKNCKSEDDT EIINYTTVGR
     IIFNEQLPKN DDGSYALEYQ NKSMTKKELV ALVDRCYKEL GQFKTTVLLD EIKRIGYKYA
     TLAGISISID EMKVPTEKEK MVREAKTKIS EIEKQAKLGL ITESERYNRI IDIWTRVTDE
     ISDIMFDEMR KEETKAYKPG QNRFNSIFMM ADSGSRGSRQ QVRQLAGMRG LMAKPQKKLT
     GGIGEIIETP IISNFREGLT VLEYFISTHG GRKGLADTAL KTAEAGYLTR RLVDVAHDVV
     VREEDCGTVN GVFIGTLRCG DEIIEKIDER VVGRTALDNV VDIVHDDLII KRGELITPKK
     AEKLVEAGID KIGIRSVLTC ESGHGVCAKC YGVNPATGEQ VEMGEAVGIL AAQSIGEPGT
     QLTLRTFHIG GAASRVVQRS EVYAENNGTV NYYNLKTIQN KDGETIVLSR NAELVYTEYP
     VYRKQIYQIP YGAVIKIYDG QTVEIRVNPI TGMKKDILIA KWDPHSKPII SEFDGTVNFV
     DVKDGVTLQR EKSKITGQIE RVIIEHSSDR RSPRIVVKKD DGSVVEYPLP VDTTLVVRDK
     DRVKSGDILA KIPQEISRTK DITGGLPRVA ELFEGRRPRN VAVVSEIDGI VHLVGPTVKG
     NVKVEVENPE TKMKKSYLVR AGRHLVVYEG DRVKEGEALS DGAINPHDIL KVKGPKEVQE
     YLVNEIQQVY RLQGVSINDK HIEIIVRQML SNVRITDSGD SHYLNGEIVS RYKYEIDRKA
     IKGKKGKAPI AHSILLGITK ASLSSDSFIS AASFQETTRI LTEAAVSGQV DYLKGLKENV
     SIGRLIPAGT GLAAVDIDDN NKFYSREQND AND