ID J6H2E1_9PORP Unreviewed; 1451 AA.
AC J6H2E1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ECO:0000313|EMBL:EJU17283.1};
GN ORFNames=HMPREF1323_1227 {ECO:0000313|EMBL:EJU17283.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU17283.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU17283.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU17283.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-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|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:EJU17283.1}.
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DR EMBL; ALKJ01000016; EJU17283.1; -; Genomic_DNA.
DR RefSeq; WP_009432736.1; NZ_ALKJ01000016.1.
DR PATRIC; fig|1125723.3.peg.711; -.
DR Proteomes; UP000004156; 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; -; 2.
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; 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; 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:UP000004156};
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 264..543
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 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 831
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"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1451 AA; 161347 MW; 12597CE47D8E63FB CRC64;
MAFKKDNKIK SNFSQIRISL ASPEEILENS SGEVLKPETV NYRTYKPERD GLFCERIFGP
VKDFECHCGK YKRIRYRGIV CDRCGVEVTE KKVRRERMGH IKLEVPIAHV WYFRSLPNKM
GYLLGLSTKK LESIIYYERY VLIQGGVLQS RINDDLTKET AAKSLDKDPN PVFTEEQYLD
YLDYLDQEYP GNAQLEDSDP EKFICKTGAE AIYDMLARLD LDALSYELRH RASTDGSQQR
KNEALKRLQV VESFRASKNV NRPEWMIMKV LPVIPPDLRP LVPLDGGRFA TSDLNDLYRR
VIIRNNRLKR MIEIKAPEVI LRNEKRMLQE AVDSLFDNSR KSSAVRSDNN RPLKSLSDSL
KGKQGRFRQN LLGKRVDYSA RSVIVVGPEL KMHECGLPKY MAAELYKPFV IRKLIERGIV
KTVKSAKKIV DRKDPVVWDI LEHVMKGHPV LLNRAPTLHR LGIQAFQPKM IEGKAIQLHP
LSCTAFNADF DGDQMAVHLP LGNEAILEAQ MLMLASHNIL NPANGAPITV PSQDMVLGLY
YITKLRPGAK GDGYTFYGVE EATIAYNEGK IDLHAPIKVY VDDVKDGEPI RHMVDTSMGR
LLVNEYVPKE VGYVNEVLGK KSLRDIIGRV IKVCGVAITA QFLDDIKNLG YYMAFKGGLS
FNLGDVIIPE EKAKLIAEGY EAVEEIMMNY SGGFITNNER YNQIIDTWTH VNSQLTGILM
KHLSEDNQGF NSVFMMMDSG ARGSKEQIRQ LSGIRGLMAK PQKSGSEGGQ IIENPILSNF
KEGLSVLEYF ISTHGARKGL ADTALKTADA GYLTRRLVDV SQDVIVTEED CGTLRGLVAT
ELTKEDNDDE VVATLYERIL GRVSVHDVIH PSTGEVLVRA GEEIREAAAE RIQASPIEQV
EIRSVLTCES KKGVCAKCYG RNLATNILVQ KGEVVGVIAA QSIGEPGTQL TLRTFHVGGV
ASNVATRNSV AAKYDGIVTF DDLRVAEVAS EDGGKPVNIV VSRMTELKIS DKNTKIVLRS
VKVPYGAKLF FAEGEEVKKG QTLFEFDPFN ALIISEVSGK VVFDNLIEGS TYRVESDEAS
GLKEMIITES KDRNVVPGIH IEDANGNLLK SYNLPVGAHV VQENHSEIHV GETLAKIPRS
MSKAGDITGG LPRVTELFEA RNPSNPAVVA EVDGVVSFGK SLKRGNREVI VTTKLGAERK
YLVPTSKQIL VQEGDSVYAG MPLSDGAITP TDILEIKGPT AVQEYIVNEV QDVYRLQGVK
INDKHFEVIV RQMMRKVEIL DPGDTLFLEQ QVVDKLEVMD ENDRLWGKVV VVDAGDSETL
SPGQIVTLRK LRDENSQLKR RDLRTVEVRE AKPATARQIL QGITRAALQT KSFMSAASFQ
ETTKVLNDAA INGKVDTLEG LKENVICGHL IPAGTGLREY KRLVVMPVSE HEQALAASSG
LDLEGDISIA G
//
