RPOC_PORCN
ID RPOC_PORCN Reviewed; 1159 AA.
AC O33431;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
DE Flags: Fragment;
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700135 / JCM 15983 / NCTC 12856 / VPB 4874;
RX PubMed=8863429; DOI=10.1099/00207713-46-4-1004;
RA Morse R., Collins M.D., O'Hanlon K., Wallbanks S., Richardson P.T.;
RT "Analysis of the beta' subunit of DNA-dependent RNA polymerase does not
RT support the hypothesis inferred from 16S rRNA analysis that Oenococcus oeni
RT (formerly Leuconostoc oenos) is a tachytelic (fast-evolving) bacterium.";
RL Int. J. Syst. Bacteriol. 46:1004-1009(1996).
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 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-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, ECO:0000305}.
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DR EMBL; X96383; CAA65247.1; -; Genomic_DNA.
DR AlphaFoldDB; O33431; -.
DR SMR; O33431; -.
DR PRIDE; O33431; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
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..>1159
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067775"
FT BINDING 398
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 400
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT NON_TER 1
FT NON_TER 1159
SQ SEQUENCE 1159 AA; 128397 MW; 726D561EEA6B904B CRC64;
VLRYRGIVCD RCGVEVTEKK VRRERMGHIA LEVPVAHIWF FRSIPNKIAY LLGIPSKKLD
AIIYYERYAV IQPGTVEGLA AGDLLTEEEY LDILDSLPEG NQDLEDDAPE KFIAKIGAEA
IYDLLCRVDL DKLSYELRAK ASKDSSQQRK KEALKRLQVV ESFRASEGYS RPEWMVMKVI
PVIPPELHTL VPLDGGRFAT SDLNELCRRV IIRNNRLRRL IEQRAPQVIL RNEKRMLQEA
VDSFFDNSSK AGAVKSDSNR PLKSLTDSLK GKQGRFRQNL LGKRVDYSGR SVIVVGPEPK
MHECGLPKYM AAELYKPFVI RKLLERGIVK TVKSARRIVD KKGPEVWDIL EHVIKGHPVL
LNRAPTLHRL GIQAFQPKLI EGKAIQLHPL ACTAFNADFD GDQMAVHLPL SNEAILEAQM
LMLASHNILN PANGAPITVP SQDMVLGLYY ITKLRKDAKG AGLVFYGREE ATIAYNDGKV
AIHAPIKVMV DDVDADGNPI RHLVETSVGR LMFNECVPQG VGYINSILGK KALRDIIGHV
IKECGIAKTA KFLDDIKDLG YQMAFKGGLS FNLSDVLIPK EKDTLIQEGF AEVDEIMSNY
NMGFITNNER YNQIIDTWTH VNTCLSGILM KQLSEDNEGF NSIFMMMDSG ARGSKDQINQ
LSGIRGLMAK PQKSGTEGRT LLENPILSNF KEGLSVLEYF ISTHGARKGL SDTALKTAEC
GYLTRRLVDV SQDVIVTEED CGTLRGLVTE EIKEGDVVIA SLYERILGRV SVHDVIHPNT
GEVIVKAGEE INEKAATIIQ DSPITNVEIR SVLTCESKKG VCAKCYGRNL SQGHMVHIGE
VVGVVAAQSI GEPGTQLTLR TFHTGGIASN IGSEKYVKAK YDGILEIDEL RTVDAKDEEG
NAYQVVVGRL AEMRVIDENT RMTLITHHIP YGSKLYFKPG DKVKKDDNIF ESDPFNAVII
AEETGKLKFE DVVENVTYKV EYDSNVSAGH KEHIIIESKD KNLSPSVSIL NSKGDILRTY
NLPVGAHFVK SNGDSVKTGD VLVKIPRSTL KGGDITGGLP RVTELFEARN PTNPAIVAEI
DGEVSLGRVR RGNREVTITS KLGEERKYLI PLSKQLLIQE NDYVRAGMPL SDGAITPADI
LAIKGPNAVQ DYIVNGVQD
