RPOC_TRIL1
ID RPOC_TRIL1 Reviewed; 1385 AA.
AC B3E7S9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Glov_1340;
OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS lovleyi).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Trichlorobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-2008) 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: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; CP001089; ACD95061.1; -; Genomic_DNA.
DR RefSeq; WP_012469407.1; NC_010814.1.
DR AlphaFoldDB; B3E7S9; -.
DR SMR; B3E7S9; -.
DR STRING; 398767.Glov_1340; -.
DR PRIDE; B3E7S9; -.
DR EnsemblBacteria; ACD95061; ACD95061; Glov_1340.
DR KEGG; glo:Glov_1340; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002420; 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..1385
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353374"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1385 AA; 154169 MW; 34DE72094C323BCD CRC64;
MEDYFTGSFF DKPKDPLHFS AIRISISSPE KIRERSFGEV KKPETINYRT FKPERDGLFC
AKIFGPTKDY ECNCGKYKRM KHRGIICEKC GVEVIPSKVR RERLGHIDLA TPVAHIWFLK
SLPSRIGNLL DITLKDLERV LYFEAFAITD PGTTPLKFCE VLSEDKFLKA QEEYGIDAFE
GGMGAEAVRK CLQALELDEL AVQLRMEMME STSEAKRKKV AKRLKVVEAF KQSGNKPEWM
ILECIPVLPP ELRPLVPLDG GRFATSDLND LYRRVINRNN RLKRLCELQA PEVIIRNEKR
MLQEAVDALF DNGRRGRAIA GPNKRPLKSL SDMLKGKSGR FRQNLLGKRV DYSGRSVIVV
GPELKLHQCG LPKKMALELF KPFIYNKLEE RGYVTTIKSA KKMVEKERPE VWDVLEEVIR
EHPVMLNRAP TLHRLGIQAF EPVLIEGKAI QLHPLVCTAF NADFDGDQMA VHLPLSIESQ
VETRVLMMST NNILSPAHGK PIIVPSQDMV LGTYYMTRER IGAKGERTTF ASPEEVRIAF
DHGEVDMQAR VKVRMIDAPD NPDEKPQLVD TTVGRIILRE VLPPQVPFSA INKVMNKKEL
SNLIDTCYRL AGNKETVILA DRLKETGFRY ANLAGISICI DDMVIPEGKQ AIIDRANEEV
QEIQNQYTEG LITDGERYNK VIDIWAKSTE EIAKEMLGNL SKEIVVDSDG KEVEIPSFNA
IHMMADSGAR GSAQQIRQLA GMRGLMAKPS GEIIETPITA NFREGLTVLQ YFISTHGARK
GLADTALKTA NSGYLTRRLV DVAQDAIITE DDCGTLDGLT VSSLTEGGEV IEHIGDRILG
RVALDDIHDP ITDEILVEAN QEIDENLVKK IEDAGLEKVK MRSVLTCQSK RGICAKCYGR
DLARGHIVNM GEAVGVIAAQ SIGEPGTQLT MRTFHIGGTA SRAAEQTSLE ARYEGLVKYI
NLHTVVNAEG FHIVMSRNGE VAVVDETGRE RERYGVVYGA KLKIAPEGSV KAGETLAEWD
PYTMPILTEV GGRVKFGDII EGVTMEEKLD DVTGLSRKEI VETKDSDKRP RIAIKDAGES
GGTIGRYYLP VGAIINVTED AVICGGDIIA KIPRETTKTK DITGGLPRVA ELFEARKPKD
FAVITEIDGK VNFGKDSKGK RKVVVTPELG EPKEYLIPKG KHISVHEGDY VRAGEPLMDG
SSNPHDILRV LGVKELAKYL VDEVQEVYRL QGVKINDKHI EVIVRQMLRR VRIKEVGDTN
LLIDDQVERY VFEEENAKAF AEGKRPATAE PLLLGITKAS LSTESFISAA SFQETTKVLT
QAAIEGKVDA LRGLKENVIM GRLIPAGTGI PRYRHLRLHV EEQTGEQAVT QLDAAPDLDA
EQQAA
