RPOC_ANADE
ID RPOC_ANADE Reviewed; 1394 AA.
AC Q2II85;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Adeh_1593;
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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; CP000251; ABC81366.1; -; Genomic_DNA.
DR RefSeq; WP_011420649.1; NC_007760.1.
DR AlphaFoldDB; Q2II85; -.
DR SMR; Q2II85; -.
DR STRING; 290397.Adeh_1593; -.
DR PRIDE; Q2II85; -.
DR EnsemblBacteria; ABC81366; ABC81366; Adeh_1593.
DR KEGG; ade:Adeh_1593; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001935; 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; 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 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..1394
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240794"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 474
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 1394 AA; 154552 MW; 297815CB2C104442 CRC64;
MKDIFNFFEK PKDPLSFSAI RISLASPDKI RQWSHGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RLGHITLATP VAHIWFLKSL
PSRIGNLLDI TLKDLEKVLY CESYIVIDPK ETTFQRGELL SEDRYQKALD EFGDDAFSAG
MGGEAVLGLL RGVGPASKEH GEGIPGLANE LRAEMKEATS DAKRKKIAKR LKVVEAFVAS
GNKPEWMMLE VIPVIPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLQELNAPDI
IIRNEKRMLQ EAVDALFDNG RRGKTITGPN KRPLKSLSDM LKGKQGRFRQ NLLGKRVDYS
GRSVIVVGPE LKLHQCGLPK IMALELFKPF IYNKLEEKGY VTTIKSAKKM VEKERPEVWD
ILDEVIREHP VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV
PLSIEAQMEA RVLMMSTNNI LSPAHGKPII VPSQDIVLGI YYMTRERAFA RGEGKVFASP
EEVRAAYDQG EVDLQAKVWV RMDGKRVETT VGRVLLYDIV PRRLSFDAIN KVMDKKQLQG
LIDLTYRLCG EKETVLLADR VRSMGYGNAT RAGISIALDN MVIPRKKVDL LERATREVDD
IQAQYTEGLI TIGERYNKVI DIWAQVTEEV AQEMMGEIGT ETAVGTGKDG KREERRQPSF
NPIYIMADSG ARGSAQQIRQ LAGMRGLMAK PSGEIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVAQDAII TEYDCGAMDG ITLGALVEGG EIIEPMGERI
LGRVALDDIL DAFSGNVLVK ANEEIDEGRV KLIENSGIDK VKIRSVLTCQ ARRGICVECY
GRDLARGRKV NIGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRRAEQST IENRNAGLIK
FNNVSVAKKH DGTLIVMNRN GEIIVTDDQG RERERYGVVY GAKLLVREGQ KVEANQLLAE
WDPYSMPIIT EVAGRVKYGD LVDGVTISEQ VDEITGLARK AVIASKDPDA RPRISIKDEE
GKTKKLANSD ADARYMLPEG ANLVVNDGDE VDAGDVIAKM PRETTKTKDI TGGLPRVAEL
FEARKPKEHA VISEIDGVVA FGKDTKGKRK VVITPEVDGK LRPDLAKEYL IGKGKHISVH
TGDRVRAGEA LMDGAANPHD ILRVLGEKEL ARWLVDEVQE VYRLQGVKIN DKHIETIVRQ
MLRRVRIVDV GDTEFLADEQ VEKFAFEEEN ERVLKAGGRA AQGEPLLLGI TKASLSTESF
ISASSFQETT KVLTEAAISG KVDYLRGLKE NVIMGRLVPA GTGLGAYKHL DIEVETPVDA
VEEAEEALAV GAEE
