RPOC_CHLT3
ID RPOC_CHLT3 Reviewed; 1499 AA.
AC B3QYL5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
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=Ctha_1179;
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX NCBI_TaxID=517418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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; CP001100; ACF13643.1; -; Genomic_DNA.
DR RefSeq; WP_012499727.1; NC_011026.1.
DR AlphaFoldDB; B3QYL5; -.
DR SMR; B3QYL5; -.
DR STRING; 517418.Ctha_1179; -.
DR PRIDE; B3QYL5; -.
DR EnsemblBacteria; ACF13643; ACF13643; Ctha_1179.
DR KEGG; cts:Ctha_1179; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001208; 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..1499
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353325"
FT REGION 1475..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 82
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 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 940
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1499 AA; 167904 MW; F39F19848254C591 CRC64;
MAFAIGTSPI KRDFTRIKIS VASPESILAR SRGEVLKPET INYRTYKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT SKSVRRERMG HISLAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV FVVINPGEPG RKQGLKMMDR LTEEQYYQII TEYEDNQDLD
DDDPDKFVAK MGGEAIKALL KRLDLDSTAK ELRRILKESQ SEQKKADALK RLKVVEAFRA
SYEPYSKEAK KKEEFSLEPP EPYRYEGNKP EYMVMEVIPV IPPELRPLVP LEGGRFATSD
LNDLYRRVII RNNRLKKLLD IRAPEVILRN EKRMLQEAVD ALFDNSRKAN AVKSGDSNRA
LKSLSDSLKG KQGRFRQNLL GKRVDYSGRS VIVVGPELRL HQCGLPKDMA IELFQPFVIR
RLVERGYAKS VKSAKKLIDR KDPAIWDVLE KVIEGHPIML NRAPTLHRLG IQAFQPVLVE
GKALQLHPLV CTAFNADFDG DQMAVHIPLS QEAQMEAMML MLSSHNLILP QSGKPVTVPS
QDMVLGVYYL TKVRKGARGE GNIFANTEDV VIAYNEGEVD LHARIFVRYD KPRDEKNDVL
SFIDAIPESK PEKRKWVKEQ LEAKTLMATT VGRVLFSQVM PETISFINKV LDKKTAKDLI
AHVISKVGTV RAEKFLDDVK GLGFNMAMRG GLSIGLSDAI VPETKKRYIK EAIKNSNKII
KEYNTGMLTE NEKYNKIVDV WQNVTNIVSD ESYQTLRKDR DGFNPLFMML DSGARGSRNQ
ARQLTGMRGL IARPQKSMSG QPGEIIENPI ISNLREGLTV LEYFISTHGA RKGLSDTSLK
TADAGYLTRR LHDVAQDVIV TEDDCGTTMG IHIRRDEEEV AGKVKFHDKL RGRYVAHDVV
DSITEQVVLK AGDLITDEIA EELRLNVGVT DVMIRSVLTC DSKRGICAKC YGTNLASGRQ
VDAGEAVGVI AAQSIGEPGT QLTLRTFHQG GAAQGGIAET EIRSQYEGQL EFENIQMVQS
KTFNEDGAEE VHDIVIRKNG VMNIVDPSTG KILKRMIVPY GAKMNCKDGD MVQKGSLLYG
VEPNSTPILA EKDGVIKFVD IEKGVTYKEE SDQQTGHVQR VIINWRSRVR TVDIREPRIQ
LLTHHGELIA SYPIPIKANL HSEDGATVHA GDVLAKVPRD LTRIGGDITA GLPRVTELFE
ARNPSDPAVV SEIDGIVTFG SQRRNNKEVK VKNAYDDERI YLVPIGKHIL VNEGDEVRAG
DPITDGSISP QDILRIQGPN AVQQYLVNEI QKVYQINAGV EINDKHLEVI VRQMLQKVQV
EDSGDTHLMP GDLIDKTTFK DVNSKIQGKV RVSEKGDARN IQEGELYAKE EIGRLNRELR
KNNRVLVTFE PAVPATSRPV LLGITSAALQ TESFISAASF QETTKVLTDA AVEGKTDFLA
GLKENVIVGK LIPAGTGLKR YRSLRISTAN LQDSYEPSQR AYQEDEYAKK EDGEIAIDD
