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Entry: I7IC51_9BURK
LinkDB: I7IC51_9BURK
Original site: I7IC51_9BURK 
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
//
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