ID J3YQH6_CARRU Unreviewed; 1287 AA.
AC J3YQH6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322,
GN ECO:0000313|EMBL:AFP84208.1};
GN ORFNames=A355_0189 {ECO:0000313|EMBL:AFP84208.1};
OS Candidatus Carsonella ruddii HT isolate Thao2000.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX NCBI_TaxID=1202539 {ECO:0000313|EMBL:AFP84208.1, ECO:0000313|Proteomes:UP000003933};
RN [1] {ECO:0000313|EMBL:AFP84208.1, ECO:0000313|Proteomes:UP000003933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT {ECO:0000313|EMBL:AFP84208.1,
RC ECO:0000313|Proteomes:UP000003933};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|HAMAP-Rule:MF_01322,
CC ECO:0000256|RuleBase:RU004279}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01322}.
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DR EMBL; CP003544; AFP84208.1; -; Genomic_DNA.
DR RefSeq; WP_014887508.1; NC_018417.1.
DR STRING; 1202539.A355_0189; -.
DR KEGG; crt:A355_0189; -.
DR PATRIC; fig|1202539.3.peg.159; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000003933; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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 NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01322};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 204..483
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 818
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1287 AA; 150000 MW; 190D160F55C6D784 CRC64;
MKNISIKIAS PNKIINWSYG EIKNSNYIDY KSLKPEINGL FCLKIFSIYN ICCNKKKCEC
NKNNKFLNLK KSHSSYRFGH LKLNYPIIHI WFLKTISNNV TNIINISNKL LDKIINFKVK
IVIKSFNKKF KKYSILLNNK IKYNIYCLTG AKAIEKLLSD NEILLDCKII KKKITICNSI
CKLFKYLNII NKIYLFYLSG NKPNWFCIKI LPIVSPKIRP LIPLSIGKFA TSDLNELYRK
IINRNLRLKN IKLLGIPKQL LINERILLQE SINALFDNEK IENPILTSSK RILKSFSNSI
KGKYGRFRQN LLGKRVDFSA RSVISVNPNL FLYQCSIPIL IALELFKPFI YFELKKKKLI
SNINFIDEYY KNNKKKIINI LKLICDKKSI LLNRAPTLHR MGIQSFKILL TQDKTIKLHP
LVCLSYNADF DGDQMAIHLP LTINSQLESN YILLSINNII SPSNGEPIIV PTQDIVMGIY
CLTFNYNYKE IYFNNILDVI SYFNINNNSF LNNILLKIYN KKIKTTIGRI ILYYSLFKNI
HIKFLNKNLK KKNLSYIIKY YFDYFDLNIT IKILDKIKKI GFFFSTLFGI SINYYDLVSI
KTNLCILKII KKIKIKKNIF SIINTIEILF LNLLIKKISP KKNKNINNLF IMLDSGSRGS
MLQIKQLIAF RGFFSKSNGD IILDPILDNL KNGLTMKNYF ISSYGARKGL TDTSLKTANS
GYLTRKLVDV LQDVVIYKIN CNTKLGIKIF ISKYNKINLL YKKIYGRVLI NDIFINNKIF
IKKNTFINNK IIFLIIKKNI KKIFIRSVIY CISSRGICSF CYGSDLSKNN IIQVGVPVGI
IAAQSIGEPG TQLTMRTFHT GGVASFSFNN YFLYNKNYGY VIYKDCKCLL NTNNEILILN
NISSVIINNN NFKEIYKLLY GERILIRNGL FIKTKIKIKN LESIFCIFSE NIGYFFFNDS
LKKFFYETDQ KYYYKTLKKT IFYIKNKNKI KKYFIPKDFF IIKEKFDFIM PGDIIAKIQI
ILKIKSSIIG GLPRLSELFE ARIPKKKALL SEIDGIVKIF NYKKFKIINI FTKYNFYKQY
YIENFRIILV NNMDYVKIGD ILSDGKPDLN DVIKLIGIEY LINYFIIEIN SIYEPQGIYI
NDKHIELVLK QMIKKVRILY SGDCFFIQND ILYLEDVLTE NINTLKYSKK ISLYERVVFG
ITKVSLDSSS FFSAASFQET SKILIDSAIR NRVDYLLGLK ENVVIGRLIP AGTGLINHIY
FLKNNIDINN KKKNLKFYIK NDFKSNN
//
