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Entry: A0A1G9V5Z8_9FIRM
LinkDB: A0A1G9V5Z8_9FIRM
Original site: A0A1G9V5Z8_9FIRM 
ID   A0A1G9V5Z8_9FIRM        Unreviewed;      1316 AA.
AC   A0A1G9V5Z8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04488502_106181 {ECO:0000313|EMBL:SDM67487.1};
OS   Dendrosporobacter quercicolus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Dendrosporobacter.
OX   NCBI_TaxID=146817 {ECO:0000313|EMBL:SDM67487.1, ECO:0000313|Proteomes:UP000214880};
RN   [1] {ECO:0000313|EMBL:SDM67487.1, ECO:0000313|Proteomes:UP000214880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1736 {ECO:0000313|EMBL:SDM67487.1,
RC   ECO:0000313|Proteomes:UP000214880};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNHB01000006; SDM67487.1; -; Genomic_DNA.
DR   STRING; 146817.SAMN04488502_106181; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000214880; 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; 2.
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; 1.
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; 2.
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:UP000214880};
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          224..503
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         783
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1013
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1020
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1023
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1316 AA;  147022 MW;  CD59A7249D559A03 CRC64;
     MLDVNNFDSM RIGLASPEQI HKWSHGEVKK PETINYRTLK PEREGLFCEK IFGPQRDWEC
     HCGKYKRIRY KGIICDRCGV EVTRSKVRRD RMGHIELAAP VSHIWYFKGI PSRMGLILDI
     SPRSLEKVLY FASYIVLDPG DTPLMKKQLL SENEYRDYRD KYGNSFKVGM GAEAIKKLLE
     ELDLDKLGRE LRQELKEVSG QRKIRAIRRL EVVEAFRKSG NMPSWMILDV VPVIPPELRP
     MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPDII VRNEKRMLQE AVDALIDNGR
     RGRPVTGPGN RPLKSLSDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHQCGLPKE
     MALELFKPFV MKKLVNAGHA HNIKSAKRMV ERVRPEVWDV LEEVIKEHPV LLNRAPTLHR
     LGIQAFEPVL TEGRALKIHP LVCTAYNADF DGDQMAIHVP LSAEAQAEAR LLMLSAHNIL
     STKDGKPVAV PTQDMVLGTY YLTIEKPGAQ GEGKIVVDIN EALLAYQHKE LSLQARIKIR
     IPGYGLVNTT LGRLIFNESL PEEIRYYYQE NGEWCLGIMM DKKQLGKLVD NCYRKFGNAK
     TAVVLDKVKS LGYSFACRAG VTVAIADIMV PPEKKDILAR TETQVDTIDK QFRRGLITDD
     ERYKKVIDLW TKATDDITGA MMNNLDRFNP VYMMANSGAR GNIQQIRQLA GMRGLMADPS
     GRIIDLPIKA NFREGLTVLE YFISTHGARK GLADTALRTA DSGYLTRRLV DVAQDVIVRE
     DDCDVVGINL IRERAKLAKS STSAIGFLRD TLLGRLLAQD VFDPKTADLI VPQDTVLDDE
     NLRLIGEAGV PEITLKGTSA QIEEDVSNAA SSETIVLGAP EEHVRQALKQ SMIREMLGKN
     TIAAIKNSLG EEIVPADTKL EEEHIEAILG SDVREVKVRN NNIKGIEVEA ITEGSAVIEH
     LKDRIIGRVA AEDIVDPETG EIIVRLNQEL DEELAERVVK VRKKVSIRSV LTCKSLYGVC
     IKCYGRNLAT GHSVDVGEAV GIIAAQSIGE PGTQLTMRTF HTGGIAGDDI TQGLPRVEEL
     FEARKPKRQA IITEIEGKVE LKEIKGMRKI TIFPETGEER VYQIPYGARM IVSDGQMVEA
     GDRLTEGSVN PHDILRVRGL KDTQRYLVYE VQKVYKSQGV EINDKHIEVM VRQMLHKVKV
     EESGDTDLLP GEYIDVNTFE EENAKAIEAG GEPSVARPIL LGITKASLAT DSFLSAASFQ
     ETTRVLTDAA IKGKVDPLLG LKENVIIGKL VPAGTGMSRY RNIKIVKPAA DIVTTE
//
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