ID RPOC_SHESW Reviewed; 1405 AA. AC A1REA8; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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}; GN OrderedLocusNames=Sputw3181_0150; OS Shewanella sp. (strain W3-18-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=351745; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W3-18-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella sp. W3-18-1."; RL Submitted (DEC-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; Evidence={ECO:0000255|HAMAP- CC 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000503; ABM23003.1; -; Genomic_DNA. DR RefSeq; WP_011787568.1; NC_008750.1. DR AlphaFoldDB; A1REA8; -. DR SMR; A1REA8; -. DR GeneID; 77267624; -. DR KEGG; shw:Sputw3181_0150; -. DR HOGENOM; CLU_000524_3_1_6; -. DR Proteomes; UP000002597; 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:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd02655; RNAP_beta'_C; 1. DR CDD; cd01609; RNAP_beta'_N; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 1.10.1790.20; -; 1. DR Gene3D; 1.10.40.90; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 2.40.50.100; -; 3. DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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 NCBIfam; TIGR02386; rpoC_TIGR; 1. DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Transcription; Transferase; Zinc. FT CHAIN 1..1405 FT /note="DNA-directed RNA polymerase subunit beta'" FT /id="PRO_0000308882" 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 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322" FT BINDING 464 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322" FT BINDING 814 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322" FT BINDING 888 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" FT BINDING 898 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; 155298 MW; B5EA18D00A1330AB CRC64; MKDLLKFLKQ QSKTEEFNGI KIGLASPDLI RSWSFGEVKK PETINYRTFK PEREGLFCAR IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIELASP VAHIWFLKSL PSRIGLMLDM TLRDIERVLY FESFVVIEPG MTSLERGQML TEETYLDALE EYGDEFEAKM GAEAVLELLR AIDLAKEIEQ MREELPSINS ETRRKKVTKR LKLMEAFFTS GNKPEWMILK VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ ESVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPT LRLHQCGLPK KMALELFKPF IYGKLEGRGL ATTIKAAKKM VEREVAEVWD VLDEVIREHP VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA RALMMSTNNI LSPANGEPVI TPSQDVVLGL YYTSRERING RGEGMAFMSV AEVEKAYATG AAELHARVKV RITETIIGDD GERTEQRRIV DTTVGRALLS LILPAGLSFD LVNQNMGKKQ ISKLLNTCYR QLGLKDTVIF ADQLMYTGFR FATISGASVG IDDMVIPDEK YTLVADAEAE VLEIQEQFQS GLVTAGERYN KVIDIWASAN EKVSKAMMEN LSTETVINRD GVEEKQASFN SIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNVL QYFISTHGAR KGLADTALKT ANSGYLTRRL VDVAQDLVVI EDDCGTHEGL TMKPLIEGGD VVEPLRERVL GRVVAVDVFY PGTEDVLAPR NTLLDEAWCD KLEEHSIDEV IVRSVITCDT DFGVCAACYG RDLARGHIIN HGEAIGVVAA QSIGEPGTQL TMRTFHIGGA ASRASAENNV QVKNSGSLKL HNAKHVTNSD GKLVIVSRSS ELAIIDELGR EKERYKVPYG TVLEKLEEAA VEAGDIIANW DPHTHPIISE VAGSIKFVDM IDGVTMTRQT DELTGLSSIV ILDVGQRGTA GKEMRPMIRL LGANGSDLMI PGTEVPAQYF LPGSAIVNLD DNAQIAVGDA LARIPQESSK TRDITGGLPR VADLFEARKP KEPAILAEIS GTISFGKETK GKRRLVITPA DGGDQYEEMI PKWRNLNVFE GEKVERGEVI ADGPEAAHDI LRLRGIHNVA NYIVNEVQDV YRLQGVKIND KHIEVIIRQM LRKCLITSAG DTEFLEGEQV EVSRVKIANR ELIAQGKVPA TFERELLGIT KASLATESFI SAASFQETTR VLTEAAVGGK SDQLRGLKEN VIVGRLIPAG TGYAYHKTRN DARAKKDEPV VVNKVTASEA EQNLADLLNM AGSQD //