ID I7IC51_9BURK Unreviewed; 1440 AA.
AC I7IC51;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:CCG19946.1};
GN ORFNames=KUM_1163 {ECO:0000313|EMBL:CCG19946.1};
OS Taylorella asinigenitalis 14/45.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Taylorella.
OX NCBI_TaxID=1091495 {ECO:0000313|EMBL:CCG19946.1};
RN [1] {ECO:0000313|EMBL:CCG19946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14/45 {ECO:0000313|EMBL:CCG19946.1};
RX PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT "Comparative genomic analyses of the Taylorellae.";
RL Vet. Microbiol. 159:195-203(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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; HE681424; CCG19946.1; -; Genomic_DNA.
DR KEGG; tat:KUM_1163; -.
DR HOGENOM; CLU_000524_3_1_4; -.
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 CDD; cd01609; RNAP_beta'_N; 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; -; 3.
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:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 236..516
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1375..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1440 AA; 159105 MW; F46BC1FAC8C24852 CRC64;
MKGILNLYGQ VSNSKDQFDS IRIGIASPDK IRSWSYGEVR KSETINYRTS KPERDGLFCG
KIFGPIKDYE CSCGKYKRKK HRGVICEKCG VEVTESKVRR ERMGHIELAS PVAHIWFLKS
LPSRLGMVLD MTLRDIERVL YFEAWCVTDP GMTPLKRGQI MTSEEYDRRT EEYGDEFEAS
MGAEAIRELL QTIDIDKEVE TLREALEVTK SDAKVKKISK RLKVIEGFQK SGIKPEWMIL
EVLPVLPPNL RPLVPLDGGR FAVSDLNKLY INVINRNNRL KRLFELKTAP EIIIRNEKRM
LQEAVDSLLD NGRRGKAMTG ANKRQLKSLA DNIKGKNGRF RQNLLGKRVD YSGRSVITVG
PQLKLHQCGL PKLMALELFK PFIHNRLYKL GIAKNFNEAK RMVESQDPQV WDILAEVIRE
HPVMLNRAPT LHRLGIQAFE PQLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQM
EVRTLLLASN NVLFPASGEP SIVPSQDTVL GLYYATRERI NGKGEGMFFS DIQEMLRAYN
NGDVGLQSRI TVRLNEYSKD ENGNYVPQLK RFQTTVGRAL LSEILPKGLP FSVLNKALKK
KEISRLINQS FRRCGLRDTV IFADKLLQSG FSLATKAGIS IAMVDMVIPK EKEEILAKAA
AEVKEIDNQY SSGLVTAQER YNNVVDIWGK AGDKVGKKMM ETLSTEPVID RFGDELTQES
FNSIYMMADS GARGSVAQIR QLAGMRGLMA KPDGSIIETP ITANFREGLN VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVTQDLV ITEQDCGTSN GYVMKALVEG GDVIEPLRDR
VLGRVAALDI LDPETQQIAI PAGTLLDEDK VELIDKLGID EVKIRTPLTC ETRHGLCAHC
YGRDLGRGYL VNRGEAVGVI AAQSIGEPGT QLTMRTFHIG GAASRASLAS AVETKSAGRI
GFAGSMRYVT NAKKERVAIS RSGEIVVYDD QNRERERHKV PYGATVLVGD GDQVNAGAQL
ASWDPLTRPI VSEYKGRVKF ENIEEGVTVA KQVDEITGLS TLVVITPKTR TGKSVLRPQI
KLLNDIGEEV KIVGSEHPVN ITFPVGALIT VRDGQDVDVG EILARIPQES QKTRDITGGL
PRVVELFEAR SPKNAGVLAD VTGNVSFGKE TKGKQRLIIT KVDGEEHEIL IPKEKQVLVH
DGQVVNQGEL IVDGPPDPHD ILRLKGIEAL AQYIVNEVQD VYRLQGVKIN DKHIEVIVRQ
MLRRVNIVDA GDTDFIPGEQ VERAVLLNEN DRMREEGKRE ATYENVLLGI TKASLSTDSF
ISAASFQETT RVLTEAAIIG KRDKLNGLKE NVIVGRLIPA GTGLAYHLAR KAASNGSSSM
GSSDMSSSSS SVVENPFEEV AGAASQAKDN AADDLGGAMS SFFTLPTTSN NNDTPDPQNQ
//