RPOC_ACICJ
ID RPOC_ACICJ Reviewed; 1388 AA.
AC A5FZX0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Acry_1951;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
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 Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ31152.1; -; Genomic_DNA.
DR RefSeq; WP_012039721.1; NC_009484.1.
DR AlphaFoldDB; A5FZX0; -.
DR SMR; A5FZX0; -.
DR STRING; 349163.Acry_1951; -.
DR PRIDE; A5FZX0; -.
DR EnsemblBacteria; ABQ31152; ABQ31152; Acry_1951.
DR KEGG; acr:Acry_1951; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000245; 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..1388
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353271"
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 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 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
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 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1388 AA; 153790 MW; 31D8E811D420E896 CRC64;
MNDLMKILGQ TGQAATFDQI RIQIASPEQI RSWSYGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKF RGIICEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
PSRIATMVEM TLKDLEKVLY FENYIVLDPY TTDLKRYQLL SEDDLYAKQD EFGEDGFKAG
IGAEAVKSIL AGIDLEAERA IMRADLKEAT SEAKRKKLVK RLKLVEAFIE SGTRPEWMIM
DVVPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIVRNEKRML
QESVDALFDN GRRGRAITGT NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELKLHQCGLP KKMALELFKP FIYAKLEKYG LATTIKAAKR MVEKERPEVW DILEEVIREH
PVLLNRAPTL HRLGIQAFEP ILIEGKAIQL HPLVCTAFNA DFDGDQMAVH VPLSIEAQLE
ARVLMMSTNN ILNPANGKPI IVPSQDIVLG LYYLSLETPA FTGVEDKEAP LFGTMGEIEH
ALDSGYLKLH DKIRARVVRT HPDGSRTTEV VPTTPGRMMI GQLLPKHHDV PFALVNQLLT
KKKVSDVIDA VYRHCGQKES VIFCDRLMGL GFRQAAKAGI SFGKDDMVIP AEKYGLLEKT
QAEVKEYEAQ YHDGLITAGE RYNKVIDAWS RCNDEVAAAM MREISRQDPG KPTNSVWMMS
HSGARGSPTQ MRQLAGMRGL MAKPSGEIIE QPILSNFKEG LTVAEYFNST HGARKGLADT
ALKTANSGYL TRRLVDVAQD CIIVTADCGT ERGLTMRAVM DGGEVVSSLS ERILGRTAAE
DVLDPADGSV IVKANELIGE IDSMHIEKLG VESVKIRSVL TCEAKVGVCA KCYGRDLARG
TPVNIGEAVG VIAAQSIGEP GTQLTMRTFH IGGAAQRGAE QSSVEASHDG TVTIRNRNVV
SNSAGAPIVM SRNCEIALND ASGRERARFR VPYGARLLVD EDQTVTRGQK LAEWDPYTLP
IITERAGLVE YADLLEGVTL VERVDEVTGL TSKVVVDYKQ SAKGADLRPR LILKDERGEV
LRLANGAEAR YFLSPDSILS VENGASVHAG DVLARIPREG SKTRDITGGL PRVAELFEAR
RPKDHAIIAE TDGRVEFGKD YKAKRRIIVK NDETGEETEY LVPKGKHVSV QEGDYVHRGD
PLVDGPRVPH DILRVLGVEA LSEYLINEIQ DVYRLQGVKI NDKHIEVVVR QMLQKIEITE
PGDTTYLVGE LVDRIEFDEE NERRLRAGER PAGGLPVLQG ITKASLQTLS FISAASFQET
TRVLTEAATA GKTDQLLGLK ENVIVGRLIP AGTGSVMSRL RSIAAGRDRS TLAATRPALP
ARDEVSAD
