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Database: UniProt
Entry: R7FEN3_9FIRM
LinkDB: R7FEN3_9FIRM
Original site: R7FEN3_9FIRM 
ID   R7FEN3_9FIRM            Unreviewed;      1198 AA.
AC   R7FEN3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN   ORFNames=BN611_00819 {ECO:0000313|EMBL:CDE13734.1};
OS   Ruminococcus sp. CAG:330.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262954 {ECO:0000313|EMBL:CDE13734.1, ECO:0000313|Proteomes:UP000018377};
RN   [1] {ECO:0000313|EMBL:CDE13734.1, ECO:0000313|Proteomes:UP000018377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:330 {ECO:0000313|Proteomes:UP000018377};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE13734.1}.
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DR   EMBL; CBIH010000215; CDE13734.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7FEN3; -.
DR   STRING; 1262954.BN611_00819; -.
DR   Proteomes; UP000018377; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   CDD; cd01609; RNAP_beta'_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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   NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01322};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000018377};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          227..506
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         797
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         871
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         878
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         881
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1198 AA;  133500 MW;  7C76B25FFD821B56 CRC64;
     MEFNTFESIK IGLASPERIR EWSYGAVERP ETINYRTQKP ERDGLFCERI FGPTKDWECH
     CGKFKKIRFK GKVCDRCGVE VTRAKVRRER MGHIELAAPV SHIWYFKGTP SRIGQMLEIS
     QKHLEEVLYF TKYIVLDVGK ESKTDLVKKQ LLSEKEYFEY REKYNDDFVA EMGAEAILKL
     LQEIDLDELS AQLKMELNGL PSGQKRVKLL KRLEIVEAFR QSGNRPEWMI LTVIPVIPPD
     LRPMVMLDGG RYATSDLNDL YRRVINRNNR LKRMLELDAP NIIVRNEKRM LQEAVDALID
     NGRHGRPVTG PNNRALKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG PGLKMYQCGL
     PKEMALELFK PFVLKRLVDT KVITNIKSAR KMVDRASAEV WDALENVIHD HPVLLNRAPT
     LHRLGIQAFE PVLVEGRALK LHPLVCSAFN ADFDGDQMAV HLPLSAEAQA EARFLMLAAN
     NLLKPSDGHP VAVPTQDMVL GSYYLTLDKD GEKGEGKIFR DINEAMMAYH EGDVSIHAKI
     KVRITKDIGE KRVSKIVDCT VGRLIFNENI PQNLGYVDRT NSDHQFDLEV SFLVGKKQLG
     DIIDRCIKIH GTTTTSEVLD KIKATGFKYS TKAALTVAVC DAEIPKEKWE IVKEADAKIE
     ELTAQYEYGY ISAKEKSSKF IAIWTKATED VTDALMNGLD KYNPIFMMAD SGARGSKAQI
     RQLAGMRGLI ANTSGATIEM PIRSNYREGL NILEYFISSR GARKGLADTA LRTADSGYLT
     RRLVDVSQDV IIREHDCGAT DGLLVYELRS GNELIEKMAE RLEGRYLVDD LYDPQTGELM
     FSKNKMITSA DAKKIVDSGV ESIKIRSVLM CRAKRGVCAK CYGANLANGN LVSVGEAVGI
     IAAQSIGEPG TQLTMRTFHT GGVAVGTGGD GDITQGLPRV EELFESRHPK NAAILSKEDG
     VVHIEEIKNQ RTIWITSDNG DKEGYPIHYN FKICVLEGQR VKKGDRLTEG SIFPGDILNI
     LGVQAVQDYI ISEVQKVYRL QGVDINDKHI EVIVRQMLRK VKIDDAGSSQ LLPGTMAERN
     EVMKINEELQ ARMDAGETDL SAVTIEPILQ GITKAASSSD SFLSAASFQE TTKALTDAAI
     RGKSDHLYGL KENVIIGKLI PAGTGLDIYN GVKVVKNDAY LDHSAAVSSA PISPSPLG
//
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