RPOC_UREPA
ID RPOC_UREPA Reviewed; 1305 AA.
AC Q9PQV5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=UU188;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30595.1; -; Genomic_DNA.
DR RefSeq; WP_010891704.1; NC_002162.1.
DR AlphaFoldDB; Q9PQV5; -.
DR SMR; Q9PQV5; -.
DR STRING; 273119.UU188; -.
DR EnsemblBacteria; AAF30595; AAF30595; UU188.
DR GeneID; 29672692; -.
DR KEGG; uur:UU188; -.
DR PATRIC; fig|273119.6.peg.195; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000423; 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..1305
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067826"
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; 147970 MW; BB3C3938B7CC866F CRC64;
MSQKGIKSLT ISIASPEQIL NWSKGEITKP ETINYKSLKP EPNGLFDESI FGPSKDYECY
CGKYRKVKHK GKICERCHVE ITESIVRRER MGHIELAAPV AHIWFTKELP SPSKISLLLD
ITYKEVDQVV YFVNYIVLDE GNNVYDGKSI FNKKEVLDLT SPKNSIRSRN KLRRTLRNIQ
ERIEDELNHE REALIQDFDY RLAVTYDQML KDSNIPFSVK DVMAFIEKHT GVRFGIGAEA
IRELLEKLNL EEEHEKIKQA IQNSPNAYDQ KTKRLLRRLE CVRWIKDSGS KPEWMVMTRI
PVTPSETRPI ISLDGGRFTT SDTNNFYRKI IIRNERLKQM QATDAPEILL DNEKRLLQEA
VDSLFDNNSR KKPVVGKDKR PLKSLSNHLK GKQGLFRQNL LGKRVDYSGR SVIVVGPELK
MYEVGIPALM ILKLFRPYII SELIRKRDEL GNEIQPICAN IKLAEQKILA QDNEIWPVVE
KVIKQRPVIL NRAPTLHRLG IQAFEPKMVD GKAIRLHPLV TTAFNADFDG DQMAVHIPLS
KEAVAEARSI LLASWHILGP KDGKPIITPT QDMILGIYYL TKEKFPQVIE EMMAKDPTQA
RVEFINNFHI FSTQDEAIRA YKLKTIRIND VIGITTKAFN NKTFSKEGIL VTTVGKIIFN
QAFPVNFPYI NDVKNLYGEN QFEIIGMHES ILDYLKAYNL KEPLTKKTLS TVIDYLYKVS
EIEVVPQTMD KIKALGFKYS MISATSISAF DIPSYDQKYE YFKETDELVS KLREFYLDGK
LTDDERYTKV VQAWSQTKDK VTHDIEKLIN SNEYKDNPIV IMAKSGARGN TSNFTQLAGM
RGLMSKSYNY DQKNNNGVIK DTIEIPIKHS FIEGLSVSEY FNSSFGARKG MTDTAMKTAK
SGYMTRKLVD STQAVVIKDH DCGTKEGIIV REIRNTKDNT SIESLKDRIV GRYSINTIYD
TKNKLIIESD KLITSEIANI IQNSGIREVE VRSPLHCASL YGVCQKCFGL DLSTNKLIET
GTAIGVIAAQ SIGEPGTQLT MRTFHTGGVA GDTNITQGFE RIKQLFDCIQ PQENEKAVIS
QVKGTVERIE KDSNTNGYNV VIKYNKDNYV NYPTRSNAVL RVKTGDEIIA GQKITEGSID
VNDLLKYAGI ENVRHYIIKE VQKVYRMQGI EISDKYIEVI ISQLTNKITI TNPGDSGLFV
GETISINEFT EVAQNMLVNK KKPPSAINQV FGLDHAPSKS GSFLSAASFQ DTKKILTDAA
ARSQKDMLIG LKENVILGNL IPAGTGLKDV EEVIAYGEEM YKKQY
