ID   RPOC_CHLTE              Reviewed;        1490 AA.
AC   Q8KG14;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=CT0156;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71404.1; -; Genomic_DNA.
DR   RefSeq; NP_661062.1; NC_002932.3.
DR   RefSeq; WP_010931850.1; NC_002932.3.
DR   AlphaFoldDB; Q8KG14; -.
DR   SMR; Q8KG14; -.
DR   STRING; 194439.CT0156; -.
DR   EnsemblBacteria; AAM71404; AAM71404; CT0156.
DR   KEGG; cte:CT0156; -.
DR   PATRIC; fig|194439.7.peg.153; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_10; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001007; 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..1490
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067729"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         69
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         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         499
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         501
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         503
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         868
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         944
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         951
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         954
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1490 AA;  166282 MW;  DE4F8541B2080D00 CRC64;
     MIFSQGSSPL KGDFSKIKFS IASPESILAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
     PTKDWECYCG KYKRVRYKGI ICDRCGVEVT TKSVRRERMG HISLAVPVVH TWFFRSVPSK
     IGALLDLSTK ELERIIYYEV YVVINPGEPG EKQGIKKFDR LTEEQYFQII TEYEDNQDLE
     DNDPAKFVAK MGGEAIHMLL KGLNLDEIAL NLRKVLKESG SEQKRADALK RLKVVEAFRK
     SYEPQKRTRK KSTGLFPEED SPELYIYEGN KPEYMVMEVV PVIPPELRPL VPLEGGRFAT
     SDLNDLYRRV IIRNNRLKKL IDIRAPEVIL RNEKRMLQEA VDALFDNSRK ANAVKTGESN
     RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHQCGLPKS MAIELFQPFV
     IRRLVERGIA KSVKSAKKLI DKKDPVVWDV LEKVIDGHPV LLNRAPTLHR LGIQAFQPTL
     IEGKAIQLHP LVCTAFNADF DGDQMAVHVP LSPEAQLEAS LLMLSSHNLI LPQSGKPVTV
     PSQDMVLGMY YLTKARFGDV GQGQLFYSME EVIIAYNEER VGLHAQIFVK YDGKVDQVSD
     PVRLVDTLVP EEQAERRAWL KSQIEQKKLL VTTVGRVIFN QHMPEEIGFI NKLINKKVAK
     ELIAQLSSEV GNVETARFLD NIKEVGFDYA MRGGLSIGLS DAIVPETKVK HIKNAQRDSA
     KIIKEYNRGT LTDNERYNQI VDVWQKTSNL VADESYEKLK KDRDGFNPLY MMLDSGARGS
     REQVRQLTGM RGLIARPQKS MSGQPGEIIE NPIISNLKEG LTVLEYFIST HGARKGLSDT
     SLKTADAGYL TRRLHDVAQD VIVTIDDCGT TRGLHVERNI EEETSGQIKF REKIKGRVAA
     RDIVDVINDK VVVKAGEIIT DELAAAIQDN IGVEEAEIRS VLTCESKVGI CAKCYGTNLS
     VHKLVEIGEA VGVIAAQSIG EPGTQLTLRT FHQGGAAQGG IAETETKAFY EGQVELEDVK
     SVEHSIITED GIEETRQIVI QKNGKLNIID PDSGKVLKRY VVPHGAHLNV EHGQMVRKEQ
     VLFSSEPNST QIIAEMPGFA KFIDIEKGVT YKEEVDPQTG FAQHTIINWR SKLRASETRE
     PRVAIVSESG EIRKTYPVPI KSNLYVEDGQ KIVPGDIIAK VPRNLDRVGG DITAGLPKVT
     ELFEARIPTD PAIVSEIDGY VSFGSQRRSS KEIRVKNDFG EEKVYYVQVG KHVLATEGDE
     VKAGDPLTDG AVSPQDILRI QGPNAVQQYL VNEIQKVYQI NAGVEINDKH LEVIVRQMLQ
     KVRVEEPGDT DLLPGDLIDR STFIEANEAV AEKVRVIDRG DAPARIIEGQ LYKQRDITKL
     NRELRRNGKS LITIEPALQA TSHPVLLGIT SAALQTESVI SAASFQETTK VLTDAAVAGK
     VDHLVGLKEN VIVGKLIPAG TGLRKYRSIR LRDNEAEEAE AVEAASDEEI