RPOC_PORG3
ID RPOC_PORG3 Reviewed; 1433 AA.
AC B2RL44;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=PGN_1570;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG34089.1; -; Genomic_DNA.
DR RefSeq; WP_012458380.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RL44; -.
DR SMR; B2RL44; -.
DR STRING; 431947.PGN_1570; -.
DR EnsemblBacteria; BAG34089; BAG34089; PGN_1570.
DR GeneID; 29256744; -.
DR KEGG; pgn:PGN_1570; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR BioCyc; PGIN431947:G1G2V-1770-MON; -.
DR Proteomes; UP000008842; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1433
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141788"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1433 AA; 160244 MW; CEA8EE6A58903233 CRC64;
MAFRKENKIK NNFSKIRITL ASPEEILENS FGEVLKPETI NYRTYKPERD GLFCERIFGP
VKDFECHCGK YKRIRYRGIV CDRCGVEVTE KKVRRERMGH IHLVVPVAHI WYFRSLPNKI
GYLLGLPTKK LDAIIYYERY VVIQPGVAEG LSQLDLLSEE EYLDKLDEIE RTHKGNQNLE
DTNPDKFIAK IGAEAIYDLL CRVDLDSISY ELRDRANTDG SQQRKTEALK RLQVVESFRA
SKGVNRPEWM VMKVIPVIPP DLRPLVPLDG GRFATSDLND LYRRVIIRNN RLKRLIEIKA
PEVILRNEKR MLQEAVDSLF DNSRKSSAVK SDNNRPLKSL SDSLKGKQGR FRQNLLGKRV
DYSARSVIVV GPELKMHECG LPKDMAAELY KPFIIRKLIE RGIVKTVKSA KKIVDRKEPV
IWDILEYVMK GHPVLLNRAP TLHRLGIQAF QPKLIEGKAI QLHPLSCTAF NADFDGDQMA
VHLPLSNEAI LEAQLLMLAS HNILNPANGA PITVPSQDMV LGLYYITKLR PNIKGHGLIF
YGPEEATIAY NEGKVDIHAP IKVYVEDYEN GELVRRMVET SVGRLMVNEY VPKKVGYVNE
VLGKKALRDI IGSVIKICGV ATTAKFLDDI KNLGYYMAFK GGLSFNLADV LIPDEKDQLI
QEGYTAVEQI MQDYSMGFIT FNERYNQIID TWTHINGRLS NVLIKQLSSD NDGFNSVFMM
MDSGARGSKE QIRQLSGMRG LMAKPQKSGA EGGQIIENPI LSNFKEGLSV LEYFISTHGA
RKGLADTALK TADAGYLTRR LVDVSHDVII TEEDCGTLRG LLTTELKQNE DVVASLYERI
LGRVSVHDII HPTTGDIIVR AGEEIREQAA QIIEDSPIEA VEIRSVLTCE SKKGVCAKCY
GRNLATNRMV QRGEVVGVIA AQSIGEPGTQ LTLRTFHVGG IASNVATENS LLSKYDGILE
FEELRAVDAT DESHQVVVSR MTELRIADPN TGIILANHNI PYGAKLFFRQ GDAVKKGDKI
IEWDPFNAVI VSEVAGTLSF EGVVENVTFK MESDETTGLK EKIIIESKDK TMAPYARIID
ENGEMLKNYS LPMGAHVVKD DGDTVKVGEI LVKIPRSVGK AGDITGGLPR VTELFEARNP
SNPAIVSEID GEIGFGKLKR GNREITVTSK LGEEKKYLIP LSKQLLVQEN DFVRAGTPLS
DGAITPADIL AIKGPTAVQE YIVNEVQDVY RLQGVKINDK HFEVIVRQMM RKVEIVDPGD
TLFLEQQVVD KFEVMEENDR IWGKKVVIDA GDSQVLKAGQ IVTARKLRDE NSMLKRKDLK
IVKVRDAKSA TASQILQGIT RAALQTKSFM SAASFQETTK VLNEAAICGK TDYLEGLKEN
VICGHLIPAG TGLRDYEKLV VMHRDDYEKA TAERKSFLSV PTAEPAMEEA PSE
