RPOC_UREU1
ID RPOC_UREU1 Reviewed; 1305 AA.
AC B5ZAZ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=UUR10_0179;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001184; ACI59983.1; -; Genomic_DNA.
DR RefSeq; WP_004026159.1; NC_011374.1.
DR AlphaFoldDB; B5ZAZ4; -.
DR SMR; B5ZAZ4; -.
DR STRING; 565575.UUR10_0179; -.
DR EnsemblBacteria; ACI59983; ACI59983; UUR10_0179.
DR GeneID; 45015729; -.
DR KEGG; uue:UUR10_0179; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002018; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1305
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141799"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 922
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 997
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1004
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1305 AA; 147790 MW; 9CD87EF857CC0586 CRC64;
MSQKGIKSLT ISIASPEQIL SWSKGEITKP ETINYKSLKP EPNGLFDESI FGPSKDYECY
CGKYRKVKHK GKVCERCHVE ITESIVRRER MGHIELAAPV AHIWFTKELP SPSKISLLLD
ITYKEVDQVV YFVNYIVLDE GNNEYDGKSI FNKKEVLDLT SPKNSIRSRN KLRRTLRNIQ
ERIEEELNHE REALIQDFDY RLAVTYDQML KDSNIPFSVK DVMAFIEKHT GVRFGIGAEA
IHELLEKLNL EEEHEKIKQA IQNSPNAYDQ KTKRLLRRLE CVRWIKDSGS KPEWMVMTRI
PVTPSETRPI ISLDGGRFTT SDTNNFYRKI IIRNERLKQM QATDAPEILL DNEKRLLQEA
VDSLFDNNSR KKPVVGKDKR PLKSLSNHLK GKQGLFRQNL LGKRVDYSGR SVIVVGPELK
MYEVGIPALM ILKLFRPYII SELIRKRDEF GNEIQPICAN IKLAEQKILA QDDEIWPVVE
KVIKQRPVIL NRAPTLHRLG IQAFEPKMVD GKAIRLHPLV TTAFNADFDG DQMAVHIPLS
KEAVAEARSI LLASWHILGP KDGKPIITPT QDMILGIYYL TKEKFPQPIE EMILKDPVQA
RIEFINHFHI FATQDEAIRA YKLKTIRIND VIGITTKAFD NKSFSKEGIL VTTVGKIIFN
QAFPTNFPYI NDVKNLYGDN QFEIIGMHES ILDYLKAYNL KEPLTKKTLS TVIDYLYKVS
EIEVVPQTMD KIKALGFKYS MISATSISAF DIPSYDQKYE YFKETDELVA KLREFYLDGK
LTDDERYTKV VQAWSQTKDK VTHDIEKLIN SDEYKDNPIV IMAKSGARGN TSNFTQLAGM
RGLMSKSYNY DQKNNSGVIK DTIEIPIKHS FIEGLSVSEY FNSSFGARKG MTDTAMKTAK
SGYMTRKLVD STQAVVIKGN DCGTKEGIIV REIRNTKDNT SIESLKDRIV GRFSINPIYD
TKNKLIIEGD KLITNEIANM IQNSGIREVE VRSPLHCSSL YGVCQKCFGL DLSTNKLIET
GTAIGVIAAQ SIGEPGTQLT MRTFHTGGVA GDTNITQGFE RIKQLFDCIQ PQENEKAIIS
QVKGTVDRIE KDSNTNGYNV VIKYNKDNFV SYPTRPNAVL RIKTGDNVVA GQKITEGSID
VNDLLKYAGI ENVRHYIIKE VQKVYRMQGI EISDKYIEVI ISQLTNKVTI TNPGDSGLFV
GETISINEFT EVAQSMLVNK KKPPSAINQV FGLDHAPSKS GSFLSAASFQ DTKKILTDAA
ARSQKDMLIG LKENVILGNL IPAGTGLKDV EEVIAYGEEM YKKQY
