RPOC_EHRCJ
ID RPOC_EHRCJ Reviewed; 1410 AA.
AC Q3YST4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Ecaj_0170;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/jb.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(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; CP000107; AAZ68221.1; -; Genomic_DNA.
DR RefSeq; WP_011304299.1; NC_007354.1.
DR AlphaFoldDB; Q3YST4; -.
DR SMR; Q3YST4; -.
DR STRING; 269484.Ecaj_0170; -.
DR PRIDE; Q3YST4; -.
DR EnsemblBacteria; AAZ68221; AAZ68221; Ecaj_0170.
DR KEGG; ecn:Ecaj_0170; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000435; 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..1410
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225533"
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 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1410 AA; 157617 MW; AEDA247B785BD035 CRC64;
MKMLDLYGYT SIAQSFDKIC ISIASPESIR AMSYGEIKDI STTNYRTFKV EKGGLFCPKI
FGPVNDDECL CGKYRKKRYR GVICEKCGVE VTSSKVRRER MGHIELVSPV AHVWFLKSLP
SRIGALLDMP LKLIESILYS GDFVVIDPIA TPLSKGEVIS ESAYNQAKDN YGEDSFLALT
GAEAIRELLV RLDLHAINAN LRTELESTTS 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 IVPSKDIVLG IYYLTLQDQA QSEDEVLFFG DFSHVEYALH
NKDVHLCSKI KYRMTYCNYD VEGNKPSYYS KIIETTPGRL ILWQIFPQHK NLTFDLINQV
LTVKEITSIV DLVYRNCGQS ETVEFSDKLM SLGFKYASQS GISFGCKDMI IPDTKTMHVD
NASDKIKEFA VQYQDGLITR SERYNKVIDE WSKCTDLIAK DMMKAISVYD EENKLNSIYM
MAHSGARGSA SQMKQLSGMR GLMAKPSGEI IETPIISNFR EGLNVFEYFN STHGARKGLA
DTALKTANSG YLTRRLVDVA QDCIVVEYDC KTHNGFAIRS VVEGGAVVET LDNIILGRVA
AVDVYNPITE ELLVKAGELI DEAKVEKIKI AGLDAVKVRS PLTCEAKKGI CALCYGRDLA
IGDVVSIGEA VGVIAAQSVG EPGTQLTMRT FHVGGTAMRG VETSNLIALL DAKAKLVNSN
VVEDKHGNKI VMSRSCEIVL LDSVGNEKMR HNIPYGARLY VNDGQFVKIT EKIAEWDPYT
MPIITEKTGI IKYMDLIDGV SINEVLDEST GISNRVVVDW KLHLQGANLR PRLVLVDDNG
NIITLSNGLE ANYFIPIGAV LNVQDGQKVH AGDVITRIPR ESIKTRDITG GLPRVIELFE
ARRPKEHAIV SDIDGYVEFG KDYYRSKRRI FIKPVDDKLT PVEYLVPKGK HTIVNEGDFV
HKGDLLMDGD PDPHDILRVL GVEALANYMI SEIQQVYRLQ GVRIDNKHIE IILRQMLQKV
EIFEPGDTMY LVGENIDMEE VIKTNNSMVK MGKSPAKYAP ILQGITRASL DTNSFVSAAS
FQETTKVLTE AAFSGKEDSL YGLKENVIVG RLIPAGTGFL MNKIKKLSLL NKEDYSMYYD
SEYQDPALLQ SDSNNFGHDL PKGNNNIVDY
