RPOC_RHOBA
ID RPOC_RHOBA Reviewed; 1429 AA.
AC Q7URW4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=RB5416;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294142; CAD74223.1; -; Genomic_DNA.
DR RefSeq; NP_866684.1; NC_005027.1.
DR RefSeq; WP_007333812.1; NC_005027.1.
DR AlphaFoldDB; Q7URW4; -.
DR SMR; Q7URW4; -.
DR STRING; 243090.RB5416; -.
DR PRIDE; Q7URW4; -.
DR EnsemblBacteria; CAD74223; CAD74223; RB5416.
DR KEGG; rba:RB5416; -.
DR PATRIC; fig|243090.15.peg.2601; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; Q7URW4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001025; 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; 1.
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..1429
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067784"
FT REGION 1407..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 83
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 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 879
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 886
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"
SQ SEQUENCE 1429 AA; 159165 MW; 499ACA2AFD4EDC99 CRC64;
MSIGETSNYD RINDYASVRI SLARPQDIKA WSFGEVKKPE TINYRTYRPE KDGLFCERIF
GPEKDWECAC GKYRGMKYKG MICDRCGVKV THSRVRRKRM GHIELAAPVV HIWFFKAMPS
RLGNLLAMKT SSLEKVIYFQ DYVVTDPKDT DLEMLQLLTE EEYRAARQQY GSGSFQADMG
AEAVRDLLNK LDLVTLSDQL RVDLAETGSK QKKKDLINRL KIVESIRDSD NRPEWMVLDV
IPVIPPDLRP LVLLDSGNFA TSDLNDLYRR IINRNNRLRK LVDLNAPEVI IRNEKRMLQQ
SVDALFDNNR CKRPVLGSSN RPLKSLTDMI KGKQGRFREN LLGKRVDYSA RSVIVVGPRL
KLHQCGLPKK IALELYQPFI IRRLKELGHA DTIKSAKKML ERKDEEVWDI LEQVITNHPV
LLNRAPTLHR MGIQAFEPTL VEGNAIHLHP LVCKGFNADF DGDQMAVHLP LSIEAQVEAH
TLMMSTNNVF APSNGKPIMS PSQDIVMGCY FMTVEMPDQK GEGMTFSTYE EVDYALAQGI
VGLHTRIKLR LPKYQKLKTD DESGEYGAII DTTPGRVRFN EMLPVGMDFY NRAMRSGDLA
KSISDCYQRL GRKATIHLLD DMMQTGFRES TRSGLSFATD DLVTPDTKLQ FIKEAEKEVM
KHKKAYDRGL MTGKERYNQV LDAWTHAREA ITADMMSAME NDIRPGGWYI NPVFLMSHSG
ARGGIEQIRQ LAGMRGLMAK PTGEIIETPI KANFREGLSV LEYFSSTHGA RKGLADTALK
TADSGYLTRK LADVAQNVVV TMHDCGTTQG ITKGVVYRGE KVEVSLAESI NGRVSLKSIV
NPVTDEVIVE ANQMITPEIA RNIEAMGLEK IQVRTPMSCD APLGVCRCCY GMDMSTGSMV
EEGMAVGIIA AQSIGEPGTQ LTMRTFHIGG SVSKQVEESD IKTSRDGEVR LTRMKAVTNA
EGRDIVLTRN GQIMLVDDRG REVESYDIPT GAMLMVKEGD KVTAGQVLCE WNPYSIPILS
EVTGKIRFED VVEGETMRLD REASGNTRMT IIDHKGDLHP QLVIEDETGR PLHAQYLPER
ATISVKEGEE VIPGKVLAEM PRETGGVSDI TGGLPRVTEI FEARKPKDPA VIAEVDGEVE
ILSERKRGKR TIIVRSESGI EREHLVPHGK HFLVHTGDIV KAGQALVDGA LVPHDILRVT
GEEAVQQYLL HEIQQVYRSQ RVEINDKHGE IIIARMLRKV KIENAGDTNL LPGSVMDRFH
FRKANQDLQK CIKIANPGDT DYTEGTIVPK EAFEQTNAEV EAMGGTPAKG KRCKSATAST
QLLGITKAAV QSNSFISAAS FQETTKVLTE AALAGKVDKL VGLKENVILG HLIPAGTGFR
IFQESEVNYR REALEELSQA PVSALEESFP LLGGDGEPAS TTSSTTEGE
