RPOC_HALHL
ID RPOC_HALHL Reviewed; 1430 AA.
AC A1WVC8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
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=Hhal_0864;
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
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;
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; CP000544; ABM61640.1; -; Genomic_DNA.
DR RefSeq; WP_041595058.1; NC_008789.1.
DR AlphaFoldDB; A1WVC8; -.
DR SMR; A1WVC8; -.
DR STRING; 349124.Hhal_0864; -.
DR PRIDE; A1WVC8; -.
DR EnsemblBacteria; ABM61640; ABM61640; Hhal_0864.
DR KEGG; hha:Hhal_0864; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000647; 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; -; 1.
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..1430
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308837"
FT REGION 1388..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 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 1430 AA; 157764 MW; C34253C6B462AE49 CRC64;
MRDLLNLFKQ PGAQLEDFDA IRIGLASPEM IRSWSYGEVK KPETINYRTF KPERDGLFCA
KIFGPVKDYE CLCGKYKRLK HRGVVCEKCG VEVTVAKVRR ERMGHIDLAS PVAHIWFLKS
LPSRIGLLLD MTLRDVERVL YFEAYIVIEP GMTPLEQGQL LTDEQYLEAV EEHGDEFDAR
MGAEAVLEIL KGMDLEAEAR RLRDDIEATG SESKIKRLSK RLKLLEAFLE SGNKPEWLIM
TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLELAAPD IIVRNEKRML
QESVDALLDN GRRGRAITGT NKRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVIVVGP
TLRLHQCGLP KRMALELFKP FIFSKLQRRG LATTIKAAKK MVERETGEVW DILDEVIREH
PVLLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCTAYNA DFDGDQMAVH VPLSLEAQLE
SRAMMMSTNN ILSPASGEPI IVPSQDVVLG IYYMTRERVN ARGEGMRLAG VEEVHRAYQT
GAAELGARVE VRIRERVFDD SGEMVERVQR RQTTIGRALL FDIVPDGLPF EAVDRELDKK
GVSGLVNACY RRVGLKGTVV FADQLMYTGF FYSTKAGVSI GVDDMEVPTD KEEALRSAEE
EVREIEDQYA SGLVTSGERY NKVVDIWAHT NDQVAGAMME KMGKETVVDA EGNETEQKSL
NSIFIMADSG ARGSAAQIRQ LAGMRGLMAK PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVSQDLVV TEEDCGTTDG LVQTPIIEGG DVVETLAERV
LGRVVAEDVA VPGSTDIAVE AGTLLDEDWV ERLERMGVDE IKVRSAVTCE TRHGVCAKCY
GRDLARGHGV NIGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRAAAVSQ VEVRNTGKAR
LHNIKTVQHH SGSYVAVSRS GELTVMDEYG RERERYKIPY GAVLSVGDED PVEAGQVVAN
WDPHTHPIVT EVDGYVRFHD FVEGVTVQRE VDEVTGLSSL VVTDPKSRGT GEHKRQVTNA
NGKVTEERVA YKDLRPMIKL VDGDGNDLNI AGTQIPAHYY LPAGAIVSLE DNAEVRVGDA
LARIPQEASK TRDITGGLPR VADLFEARKP KEPAILAEAS GTVGFGKETK GKQRLIITKA
DGETHEELIP KWRNVTVFEG EHVEKGETIA DGEPNPHDIL RLLGVTKLAE YIVQEIQDVF
RLQGVGINDK HIEVIVRQML RKTIVSDPGD SLHLKGEQVD RAKLLEENEQ LQAQDKQPAQ
WEPSLLGITK ASLSTESFIS AASFQETTRV LTEAATRGIR DDLRGLKENV IVGRLIPAGT
GFAYHAARRQ EAPAPAATPE QQAEEVFASL GQGEGEGPSP SDEASGPEVE
