RPOC_FLAJ1
ID RPOC_FLAJ1 Reviewed; 1436 AA.
AC A5FIJ4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Fjoh_1944;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ04976.1; -; Genomic_DNA.
DR RefSeq; WP_012024016.1; NZ_MUGZ01000012.1.
DR AlphaFoldDB; A5FIJ4; -.
DR SMR; A5FIJ4; -.
DR STRING; 376686.Fjoh_1944; -.
DR PRIDE; A5FIJ4; -.
DR EnsemblBacteria; ABQ04976; ABQ04976; Fjoh_1944.
DR KEGG; fjo:Fjoh_1944; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006694; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1436
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353366"
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 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 829
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1436 AA; 160128 MW; B5160C65E2DDA94E CRC64;
MMNNRNNNKD KNPVKRFNKI SIGLASPESI LKESRGEVLK PETINYRTHK PERDGLFCER
IFGPVKDFEC ACGKYKRIRY KGIICDRCGV EVTEKKVRRD RVGHINLVVP IAHIWYFRSL
PNKIGYILGL PSKKLDMIIY YERYVVIQAG IAKNADGESL QRLDFLTEEE YLNILDTLPQ
ENQYLDDLDP NKFVAKMGAE CIMDLLARID LDALSYELRH SANNETSKQR KTEALKRLQV
VESFRESNEN RENRPEWMIM KVVPVIPPEL RPLVPLDGGR FATSDLNDLY RRVIIRNNRL
KRLMEIKAPE VILRNEKRML QESVDSLFDN TRKASAVKTE SNRPLKSLSD SLKGKQGRFR
QNLLGKRVDY SARSVIVVGP ELKLYECGLP KDMASELYKP FVIRKLIERG IVKTVKSAKK
IIDKKEPVVW DILENVIKGH PVLLNRAPTL HRLGIQAFQP KLIEGKAIQL HPLVCTAFNA
DFDGDQMAVH LPLGPEAILE AQLLMLASHN ILNPANGAPI TVPSQDMVLG LYYMTKERIS
TEDHIILGQD LTFYSAEEVN IALNEGRLEL NARVKIRAKD FNDAGELVYK IIQTTAGRVL
FNEVVPEAAG YINDVLTKKN LRDIIGHILS VTDVPTTAAF LDNMKDMGYK FAFRGGLSFS
LGDIRIPEQK TKLIADAREQ VEGISTNYNM GLITNNERYN QVIDVWTSAN AQLTELAMKN
IREDQQGFNS VYMMLDSGAR GSKEQIRQLT GMRGLMAKPK KSTAGGGEII ENPILSNFKE
GLSILEYFIS THGARKGLAD TALKTADAGY LTRRLHDVSQ DVIVNIEDCG TLRGVEVAAL
KKNEEIVESL GERILGRVAL QDVINPLTNE VMVQSGQQIT EAIVKTIEAS PIEKVEVRSP
LTCEALKGIC AKCYGRNLAT GKMTQRGEAV GVIAAQSIGE PGTQLTLRTF HVGGVAGGIS
EESSIVTRFA GRLEIEDLKT VKGEDSEGNA VDIVVSRSTE LKLVDEGTGI VLNTHNIPYG
SSIFVKDGET VGKGTVICKW DPYNGVIVSE FTGKIAYEDL EQGQSFMVEI DEQTGFQEKV
ISEARNKKLI PTLLVYGKEG ELIRSYNLPV GAHLMVENGE KIKAGKVLVK IPRRSSKAGD
ITGGLPRITE LLEARNPSNP AVVSEIDGVV SFGKIKRGNR EIVIESKFGE IKKYLVKLSS
QILVQENDFV RAGVPLSDGA ITPDDILRIQ GPAAVQQYLV NEIQEVYRLQ GVKINDKHFE
VVIRQMMRKV KVEDPGDTLF LEDQLIHTKD FILQNDKLYG MKVVEDAGDS SVLKPGQIIS
PRELRDENSL LKRTDKNLVV ARDVITATAT PVLQGITRAS LQTKSFISAA SFQETTKVLN
EAAVAGKVDD LEGLKENVIV GHRIPAGTGM REYDNTIVGS KDDYNEMMAN KEEYIY
