RPOC_EHRRG
ID RPOC_EHRRG Reviewed; 1411 AA.
AC Q5FFD8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=ERGA_CDS_01660;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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; CR925677; CAI27618.1; -; Genomic_DNA.
DR RefSeq; WP_011255345.1; NC_006831.1.
DR AlphaFoldDB; Q5FFD8; -.
DR SMR; Q5FFD8; -.
DR PRIDE; Q5FFD8; -.
DR EnsemblBacteria; CAI27618; CAI27618; ERGA_CDS_01660.
DR KEGG; erg:ERGA_CDS_01660; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; ERUM302409:ERGA_RS00860-MON; -.
DR Proteomes; UP000000533; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1411
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225534"
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 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 84
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 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 809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 883
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1411 AA; 157171 MW; 6C53AEF8B35E3338 CRC64;
MKMLDLYGYT SIAQSFDKIC ISIASPESIR AMSYGEIKDI STTNYRTFKV EKGGLFCPKI
FGPVNDDECL CGKYRKKRYR GVICEKCGVE VTSSKVRRER MGHIELVSPV AHVWFLKSLP
SRIGALLDMP LKLIESILYS GDFVVIDPIA TPLSKGEVIS ESAYNQAKDN YGEDSFIALT
GAEAIRELLV RLDLHAINAN LRSELESTTS EMKRKKIVKR LRIVENFINS GNKPEWMILT
VIPILPPDLR PLVSLENGRP AVSDLNHHYR TIINRNNRLG KLLKLNPPAI MIRNEKRMLQ
EAVDALFDST RRSYVSNKAG SVGYKKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
NLKLHQCGLP KKMALELFKP FICSKLKMYG IVPTVKLANK MIQNEKPEVW DILDEVIHEH
PILLNRAPTL HRLGIQAFDP VLIEGKAIQL HPLVCSAFNA DFDGDQMAVH IPLSLEAQLE
ARILMMSTNN ILSPSNGKPI IVPSKDIILG IYYLTLQDYV EPEEILFFGD FSHVEYALHN
KDIHICSKIK YKMNYCTDSS DGSGPTYYSK IVETTPGRLM LWQIFPEHKN LTFDLVNQVL
TVKEITAIVD LVYRSCGQSE TVEFSDKLMS LGFRYASQSG ISFGRMDMII PDTKTMHVDN
ASEKIKEFAV QYQDGLITKS ERYNKVIDEW SKCTDLIAKD MMKAISVYDE ESKLNSIYMM
AHSGARGSAS QMKQLAGMRG LMAKPSGEII ETPIISNFRE GLNVFEYFNS THGARKGLAD
TALKTANSGY LTRRLVDVAQ DCIVVEYDCK THNGFAMRSV IDGGTVVETL DNIILGRVAA
VDIYNPITEE LLVNAGELID EAKVEKIRIA GLDAVKVRSP LTCEAKKGIC ALCYGRDLAI
GDVVSIGEAV GVIAAQSVGE PGTQLTMRTF HVGGTAMRGV ETSNLIAMLD AKVKLVNSNV
VEDKYGNKIV MSRSCDVVLL DSVGNEKMRH SVPYGARLYV NDGQLVKITE KIADWDPYTM
PIITEKTGII KYMDLIDGVS INEVLDESTG ISNRVVVDWK LHLQGANLRP RLVLVNDNGD
IITLSSGLEA NYFIPIGAVL SVQDGQKVHA GDVITRIPRE SIKTRDITGG LPRVIELFEA
RRPKEHAIVS DIDGYVEFGK DYYRSKRRIF IKPVDDKLSP VEYLVPKGKH TIVNEGDFVH
KGDLLMDGDP DPHDILRVLG VEALANYMIA EIQQVYRLQG VRIDNKHIEV ILRQMLQKVE
IFEPGDTMYL IGENVDVEEV LKTNSNMEKI GKSPAKYIPI LQGITRASLD TNSFVSAASF
QETTKVLTEA AFSGKEDSLY GLKENVIVGR LIPAGTGFLM NKIKKLSLLN KDDYSMYYNS
EYQDLASIEA GHACSVSPSQ GVSDTSGAVD Y
