RPOBC_HELHP
ID RPOBC_HELHP Reviewed; 2894 AA.
AC Q7VJ82;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bifunctional DNA-directed RNA polymerase subunit beta-beta';
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoBC; OrderedLocusNames=HH_0361;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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_01321, 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_01321,
CC 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/beta' and
CC 1 omega subunit. When a sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- MISCELLANEOUS: Fusion of rpoB and rpoC occurs naturally in Helicobacter
CC species and at least some Wolbachia; the protein has been artificially
CC split in two in H.pylori. The split protein seems to function normally.
CC {ECO:0000250|UniProtKB:O25806}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RNA polymerase
CC beta chain family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RNA polymerase
CC beta' chain family. {ECO:0000305}.
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DR EMBL; AE017125; AAP76958.1; -; Genomic_DNA.
DR RefSeq; WP_011115204.1; NC_004917.1.
DR SMR; Q7VJ82; -.
DR STRING; 235279.HH_0361; -.
DR PRIDE; Q7VJ82; -.
DR EnsemblBacteria; AAP76958; AAP76958; HH_0361.
DR KEGG; hhe:HH_0361; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_0_1_7; -.
DR OMA; QTEKIDD; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002495; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
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; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
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; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
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; 2.
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 Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 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..2894
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000048003"
FT REGION 1..1378
FT /note="DNA-directed RNA polymerase subunit beta"
FT REGION 1385..2894
FT /note="DNA-directed RNA polymerase subunit beta'"
FT BINDING 1450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1853
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2894 AA; 324320 MW; 4566D973781FA77B CRC64;
MANFTKLKNR LRADFTKNPQ SIDVPNLLLL QRNSYDDFLC VDSDKESGIE RVFKSVFPIQ
DSQNRITLEY VSCKFGKPKY TTNEAMVRGV TYAVSLQIKI RLVLWEKDEK TGERLGIKDA
KEQNIFVRDI PLMTDRTSFI INGVERVVVN QLHRSPGVIF KEEESSASSN KLIYTGQIIP
DRGSWLYFEY DSKDVLYARI NKRRKVPVTI ILRAMGYSKQ DILKIFYPLQ RVKYKKGKYL
IPFDVDSIGN RAEFDIKDAK GNLLVSSGKR LSTKKIKELK EAKIDLIEYP LENLTNKFLA
EPIINAQGEV LFDTLTQLDE SKLKKLLELK INEFVIANAS AAGVDNSIIN SFMADAESLK
MLRQSEKIDD ENELAAIRIY KVMRPGEPVT KEVAKSFVRQ LFFDPERYDL TRVGRMKMNH
KLQINVPDYV TVLTHEDIIR TIQYLLKVKN GLGKIDDRDH LGNRRIRSIG ELLANELHTG
LVKMQKAIRD KLTSLSGAFD TIMPHDLING KMITSTIMEF FTGGQLSQFM DQTNPLSEVT
HKRRLSALGE GGLVKDRVGF EARDVHPTHY GRICPIETPE GQNIGLINTL STYTRVNDLG
FIEAPYRKVE NGIVSQEIVY LTAAQEEGIV IAPASTAVDK NGHIIEDLIE TRKDGEIILS
EKSRVQLIDL SPRMLVGVAA SLIPFLEHDD ANRALMGSNM QRQAVPLLKP DAPVVGTGIE
QIIARDSWEA TKATRSGVVE RVDAKNIYIL GEDDNGAYID HYHLGKNLRT NQNTCFSQQP
IVRQGDRVEQ GQIIADGPSM DNGELALGKN IRVAFMPWNG YNFEDAIVVS ERLIKEDAFT
SIHIYEKEIE ARELKHGLEE ITADIPGTKE AETAHLDESG IVRIGTYVSA GMILVGKVSP
KGEVKPTPEE RLLRAIFGEK AGHVVNKSLY CPPSLEGTVV DVKIFTKKGY EKDARAISAY
EEEKRVLDIE HHDRLTMIQQ EETLRISLML SKEKLLSEVK VADKVFKKGA QIPKEELSVL
NPFILSTLIK HYPKEIQTRY EQIKTNFLEQ KKTLGEEHEE KLSILEKDDI LPSGVVKLVK
IYIATKRKLK VGDKMAGRHG NKGIVSNIVP MVDMPYTADG EPVDIVLNPL GVPSRMNIGQ
ILEVHLGLVG KRLGQQIQEI LSSQSKQWLD TLRSKMIEIA QVVNSDDKSM IEFLKNLDNE
ALLAYARDWS NGVKFAIPVF EGIEQEKFDK LFSLVKVDMD GKTELYDGKT GEKMRERVNV
GYMYMLKLHH LVDEKVHARS TGPYSLVTQQ PVGGKALFGG QRFGEMEVWA LEAYGAAHTL
KEMLTIKSDD TEGRRGAYKA ITKGEHVGES EIPETFYVLT KELQSLALDV NIYGDEQDEN
GMPVPIAIKE DERPKDFSSF QLVLASPEKI LSWSNGEVKK PETINYRTLK PERDGLFCTK
IFGPVRDYEC LCGKYKKMRY KGIVCEKCGV EVTKAKVRRS RMGHIELVAP VAHIWYVSSL
PSRIGTLLGV KMKDLERVLY YEAYIVKSPG EAFYDNEGSK PILKYDVLNE EQFQSINQRF
EHTGFVAQMG GEAIKELLEE LDLILLLNTL REEIRSTNSE AKKKTIVKRL KVVESFINSG
NRPEWMMLTI LPVLPPDLRP LVALDGGKFA VSDVNDLYRR VINRNQRLKR LIELDSPEII
VRNEKRMLQE AVDALFDNGR NANAVKGANK RPLKSLSEII KGKQGRFRQN LLGKRVDFSG
RSVIVVGPNL KMNQCGLPKN MALELFKPHL FAKLEEKGYA TTLKQAVKMV NQKTNEVWEC
LQEIVNGYPV LLNRAPTLHK QSIQAFHPKL IDGKAIQLHP LVCSAFNADF DGDQMAVHVP
LSQEAIAECK ILMLSSMNIL LPASGKAVAV PSQDMVLGLY YLSLEKKGVK GEHKILASID
EIVMAIEMGE LDINARIKTV HNRRVIDTTA GRMILSSILP DFVPLNLWNQ TMKKKDIGTL
IDYVYKEGGL GITATFLDNL KNLGFKYATK AGISISAADI IIPHNKATMI DEAKKEIKRI
QGEFEQGLLT AQERYNKSID IWTETSEKMG KLMMEKVKND KEGFNSIYMM ADSGARGSEA
QIRQLSAMRG LMAKPDGTII ETPITSNFKE GLNVLEYFNS THGARKGLAD TALKTANAGY
LTRKLIDVSQ NMKVTIEDCG THEGVEITDI TVGSDMIEPL EERVVGRVLA RDVIDPIANE
ILLSEGVLID STMARRIKEA NVKSVMIRTP VTCKAQKGVC AKCYGLNLGE SKMVKPGEAV
GVLAAQSIGE PGTQLTLRTF HVGGTASRST EEKQIVAKKE GFIRYYNIRT YTNSKGQKIV
ANRRNAAILV VEPRIKAEFD GELEVENVHD EVHITIVGDK KRSETYRLRK DDVAKQNELA
GVAGKIEGKL LVPHESGYKV KAGGSIVDTI MDSWNIPTRI PYGSELKVED NAPISQKITA
KEKGIVKFYT LRADTLERNH NVKAGMVVSE KGMFAVIADQ NDREAIRHYI ARTSKILVDD
NSEVDINTLI SEPTSTEQIV VAEWDAYSEP IIADQAGIVS FRDIIAGLTV SEQEDENTHQ
KNFVINEYVP AGYKPMLVVT TKDGKEISYR LESRTSIAVN DGDKVEIADI IAKVPKALAK
SKDITGGLPR VTELFEARKP KDTAILSELD GTVSFGKPIR GKERIIITAA DGRVAEYAVD
KNKKILVHEQ EFIHAGEAMT DGVISSHDIL RISGEKELHK YIVSEVQQVY RRQGVSIADK
HIEIIVSQML RQVKIVDSGN TKFIEGDLAS KRHFKEENER ILSIGGEPAV AEPVLLGITR
AAIGSDSIIS AASFQETTKV LTEASIAAKK DTLDDLKENV VLGRMIPVGT GLYKNKKFHY
RCEKQEEYEE DEEE
