RPOC_AZOPC
ID RPOC_AZOPC Reviewed; 1405 AA.
AC B6YPZ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CFPG_005;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP010656; BAG83268.1; -; Genomic_DNA.
DR RefSeq; WP_012573029.1; NC_011565.1.
DR AlphaFoldDB; B6YPZ6; -.
DR SMR; B6YPZ6; -.
DR STRING; 511995.CFPG_005; -.
DR PRIDE; B6YPZ6; -.
DR EnsemblBacteria; BAG83268; BAG83268; CFPG_005.
DR KEGG; aps:CFPG_005; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000723; 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; -; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1405
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141758"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1405 AA; 158028 MW; 13ACC3EF07DF0E6B CRC64;
MAFRKENKVK SFTRIFISLA SSDNILAQSS GEVLKPETIN YRTYRPERDG LFCERIFGPI
KDYECHCGKY KRIRYKGVVC DRCGVEVTEK RVRRERMGHI QLVVPVVHIW YFRSLPNKIG
YLLGLSSKKL DAIIYYERFV VIQPGITDKK VCDLLSEEEY LEVLDGLPVE NQRLDDINPD
KFIAKMGGEA IYDLLSRLEL DSLSYELRHK IDNDTSQQRK IDALKRLQVI ESFRSSKNKN
RPEWMVIGVI PVIPPELRPL IPLDGGRFAA SDVNDLYRRV IIRNNRLKRL IDIDAPDVIL
RNEKRMLQEA VDSLFDNSRK SSAVKTDANR PLKSLSDSLK GKQGRFRQNL LGKRVDYSAR
SVIVVGPELK MHECGLPKGI AAELYKPFII RKLMDRGVVK TVKSAKKLVD GRDPIIWDIL
EYVMKGHPVL LNRAPTLHRL SIQAFQPKLI EGKAIQLHPL SCTAFNADFD GDQMAVHLPL
GNEAILEAQM LMLASHNILN PANGTPITIP SQDMVLGLFY ITKMRRGAKG EGLKFYGTEE
AIIAYNEGKV DIHAFVKVYV DDIDENGTPI NHIIETSVGR VIVNGFVPKA VGFVNEELSK
KSLRSVISDV IKTCGVSRTA QFLDDIKDLG YMMAFKGCLS FNLDNVIVPK EKETFVQEGY
KEIEEILANY NMGIITYNER YNQIIDTWTH VNSRLSDALM KQLREDDQGF NPVFMMLESG
ARGSKEQIRQ LSGMRGLMAK PQKSVMGGGQ IIENPILSNF KEGLSVLEYF ISTHGARKGL
ADTALKTADA GYLTRRLVDV SHNVIINEED CGTLRGLIAT ELRKNEDVVV SLYERILGRV
SVCDVQHPES RKIIVYAGEE ISEDKALAIQ NSSIERVEIR SVLTCESKKG VCVKCYGRNL
ATGSIVQIGE AVGVIAAQSI GEPGTQLTLR TFHVGGIASN IATESSVVSK YDGILEIDEL
RTVEVVDEIN NRHLIVVSRL AEMRIIDTRT KIVLATYNIP YASKLFFNDR DEIKKGDLLF
EWDAFNASIV SEVAGRFHLE NVIENITYKN EYDEQTGLKE KVIIESRDKT KIPVIHILDE
NGEIRRIYNL PLGAHITKEE KDVIRVGEVL VKIPRTVGKT GDITGGLPRV TELFEARNPS
NPAVVSEIDG EISFGKVKRG SREVIVTSKN GDYRTYLVSL SKQILVQEND YIRAGMPLSD
GIIAPSDILA VNGPTAVQEY IVNEIQDVYR LQGVKINDKH FEVIVRQMMR KVEIIEAGDT
KFVARQLVDR DEVSEENDHI WDKKVVVNVG DSSNVKQGQI ITMRKLREEN SILKRRDLRL
IEVRDSIPAT VMQILQGITR ASLQTSSFIS AASFQETAKV LNEAAIKGKV DKLVGMKENV
ICGRLIPAGT GLKEYDKIMV ETTME
