ID A0A099BXA0_9BACT Unreviewed; 1439 AA.
AC A0A099BXA0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF0671_03230 {ECO:0000313|EMBL:KGI60916.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60916.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI60916.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60916.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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|HAMAP-Rule:MF_01322,
CC 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:KGI60916.1}.
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DR EMBL; JRPT01000014; KGI60916.1; -; Genomic_DNA.
DR RefSeq; WP_036896667.1; NZ_JRPT01000014.1.
DR eggNOG; COG0086; Bacteria.
DR Proteomes; UP000029732; 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; -; 3.
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; 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:UP000029732};
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 257..536
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 824
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1439 AA; 159616 MW; 99B728BDB32B7591 CRC64;
MAFKKDSKVK NNFTKITIGL ASPEEILENS YGEVTKPETI NYRTYKPERD GLFCERIFGP
TRDYECACGK YKRIRYKGIV CDRCGVEVTE KKVRRERSGH IELVVPVAHI WYFRSLPNKI
GYLLGMPTKK LDTVIYYEKY IVIKPGAMEG RTDADGNEVN GSHKMDLLSE EEYLDILDNQ
IDSNNEYLDD SDPNKFIAKM GAEAVYDLLG DLDLDSLSYE LRDRANNDSS QQRKTEALKR
LQVVEAFRAS KDVNHPEWMI MKIIPVIPPE LRPLVPLDGG RFATSDLNDL YRRVIIRNNR
LKRLMEIKAP EVILRNEKRM LQEAVDSLFD NSRKASAVKS ESNRPLKSLS DSLKGKQGRF
RQNLLGKRVD YSARSVIVVG PELKMGECGL PKLMAAELYK PFIIRKLIER GIVKTVKSAK
KIVDRREPVI WDILENVMKG HPVMLNRAPT LHRLGIQAFQ PKLIEGKAIQ LHPLACTAFN
ADFDGDQMAV HLPLSNEAIL ETQVLMLQSH NILNPANGAP ITVPSQDMVL GLYYITKLRP
GAKGEGLTFY GPEEALVAYN EKKCDLHAPV KVVVKDLVNG QLEPRMVETS VGRVVVNQII
PEEIGYFNDI ISKKTLRGII ADVIKAVGMA RACEFLDGIK NLGYHMSYVA GLSFNLDDII
IPEEKKAIVA RGQSEVDQIK TNYEMGFITD TERYNQVIDA WTHVNNDLGN ILMKEMTEAD
QGFNAVFMML DSGARGSKDQ IKQLSGMRGL MAKPQKAGAE GAQIIENPIL SNFKEGMSVL
EYFISSHGAR KGLADTAMKT ADAGYLTRRL VDVSHDVIIS EEDCGTLRGL VCTALKNGDE
VISTLYERIL GRVSVHDILE PTTGELIVHA GEEITEDKAQ AIENSPIESV EIRSVLTCES
KHGVCMKCYG RNLATARMVQ LGEAVGVIAA QAIGEPGTQL TLRTFHAGGV AGNAAANASI
VAKNNSKLEF DELRTVPFVE ESDSDVKCQM VVSRLAEVRF VDPNTNIVLG TLNVPYGSIL
YNKTGDTVKK GDVVAKWDPF NAVIVSEYAG TLKFNDVVEG RTYHAETDET TGLTEKIITD
SKDKTMVPTC DILNSKGEVL GTYNLPVGGH VVVEDGQAIK TGETLVKIPR AVGGAGDITG
GLPRVTELFE ARNPSNPAVV SEIDGEVTMG KVKRGNREII VTSKTGDQKK YLVSLSKQIL
VQEHDAVRAG TPLSDGVITP SDILAIKGPT AVQEYIVNEV QDVYRLQGVK INDKHFEIIV
RQMMRKVHID DPGDTTFLEQ EMVDKLDFAE ENDRIWGKKV VVDAGDSETL KPGQIVSARK
LRDENSSLKR RDLKLVQVRD AVAATSTQML QGITRAALAT KSFMSAASFQ ETTKVLNESA
IRGRVDRLEG MKENVICGHL IPAGTGLRQW DKLIVGSKEE FERMQANRRN VLDFAEQEA
//
