RPOC_FLAPJ
ID RPOC_FLAPJ Reviewed; 1438 AA.
AC A6GYT9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=FP1175;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL43262.1; -; Genomic_DNA.
DR RefSeq; WP_011963311.1; NC_009613.3.
DR RefSeq; YP_001296073.1; NC_009613.3.
DR AlphaFoldDB; A6GYT9; -.
DR SMR; A6GYT9; -.
DR STRING; 402612.FP1175; -.
DR PRIDE; A6GYT9; -.
DR EnsemblBacteria; CAL43262; CAL43262; FP1175.
DR GeneID; 66553079; -.
DR KEGG; fps:FP1175; -.
DR PATRIC; fig|402612.5.peg.1192; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006394; 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..1438
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308834"
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 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 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1438 AA; 160606 MW; 5FF5783E28EB5929 CRC64;
MMENRNNNNN RDKNPVKRFN KISIGLASPE SILAESRGEV LKPETINYRT HKPERDGLFC
ERIFGPVKDF ECACGKYKRI RYKGIVCDRC GVEVTEKKVR RDRVGHINLV VPIAHIWYFR
SLPNKIGYIL GLPSKKLDMI IYYERYVVIQ AGIAQNAEGE SIKRLDFLTE EEYLNILDTL
PADNQYLDDF DPNKFVAKMG AECIMDLLAR INLDELSYDL RHKANNETSK QRKTEALKRL
QVVESFRESN KNRENRPEWM IMKVVPVIPP ELRPLVPLDG GRFATSDLND LYRRVIIRNN
RLKRLMEIKA PEVILRNEKR MLQESVDSLF DNTRKASAVK TESNRPLKSL SDSLKGKQGR
FRQNLLGKRV DYSARSVIVV GPELRLFECG IPKDMAAELY KPFVIRKLIE RGIVKTVKSA
KKIIDKKEPV VWDILENVIK GHPILLNRAP TLHRLGIQAF QPKLIEGKAI QLHPLVCTAF
NADFDGDQMA VHLPLGPEAI LEAQLLMLAS HNILNPANGA PVTVPSQDMV LGLYYMTKER
LTTEGHIILG QDLVFYSAEE TNIALNEGRV ELNARVKIRA KDFNEEGELV YKIIQTTAGR
VLFNEVVPEA AGYINDVLTK KNLRDIIGKI LAVTDVPTTA AFLDNIKDMG YKFAFKGGLS
FSLGDIRIPE QKTQLIADAR AQVEGISGNY NMGLITNNER YNQVIDIWTS ANAQLTELAM
KNIREDQQGF NSVYMMLDSG ARGSKEQIRQ LTGMRGLMAK PKKSTAGGGE IIENPILSNF
KEGLSILEYF ISTHGARKGL ADTALKTADA GYLTRRLHDV SQDVIVNIED CGTLRGVEVS
ALKKNEEIVE SLGERILGRV VLQDVVNPLT NDILVHAGEQ ITEAIMKVIE NSPVEKVEVR
SPLVCEATKG ICAKCYGRNL ATGKMTQRGE AVGVIAAQSI GEPGTQLTLR TFHVGGVAGG
ISEESNILAK FAGRLEIEDL KTVKGEDGEG NLVDIVISRS TEMKLIDQKT GILLATNNIP
YGSSIYVNDA QVVEKGDVIC KWDPYNGVIV SEFTGKIAYE DLEQGQSFMV EIDEQTGFQE
KVISEGRNKK LIPTLLVYGK NDELIRSYNL PVGAHLMVND GEKIKAGKIL VKIPRRSSKT
GDITGGLPRI TELLEARNPS NPAVVSEIDG VVSFGKIKRG NREIVIESKF GEIKKYLVKL
SSQILVQEND FVRAGVPLSD GAITPDDILR IQGPAAVQQY LVNEIQEVYR LQGVKINDKH
FEVVIRQMMR KVRVQDPGDT LFLEDQLIHT KDFIVENDKL YGMKVVEDSG DSSNLKAGQI
ITPRELRDEN SLLKRTDKNL VIARDVITAT ATPVLQGITR ASLQTKSFIS AASFQETTKV
LNEAAVAGKI DYLEGLKENV IVGHRIPAGT GMREYDHTIV GSKEEYNDLM VAKEEFNY
