ID C3XD74_9HELI Unreviewed; 2883 AA.
AC C3XD74;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|HAMAP-Rule:MF_01322};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE Includes:
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 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 Synonyms=rpoB {ECO:0000256|HAMAP-Rule:MF_01321};
GN ORFNames=HRAG_00020 {ECO:0000313|EMBL:EEO22963.1};
OS Helicobacter bilis ATCC 43879.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=613026 {ECO:0000313|EMBL:EEO22963.1, ECO:0000313|Proteomes:UP000005085};
RN [1] {ECO:0000313|EMBL:EEO22963.1, ECO:0000313|Proteomes:UP000005085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43879 {ECO:0000313|EMBL:EEO22963.1,
RC ECO:0000313|Proteomes:UP000005085};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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_01321, 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_01321, 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_01321, ECO:0000256|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RNA polymerase
CC beta' chain family. {ECO:0000256|ARBA:ARBA00009839}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RNA polymerase
CC beta chain family. {ECO:0000256|ARBA:ARBA00007616}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEO22963.1}.
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DR EMBL; ACDN02000002; EEO22963.1; -; Genomic_DNA.
DR RefSeq; WP_005216504.1; NZ_KI392032.1.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_0_1_7; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000005085; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
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; -; 4.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1100.10; -; 2.
DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 2.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 2.
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 NCBIfam; TIGR02013; rpoB; 1.
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 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 2.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01321};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, 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_01321}; Reference proteome {ECO:0000313|Proteomes:UP000005085};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01321};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01321}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 1621..1900
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 1447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1846
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1850
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2883 AA; 323264 MW; 06242EE9A9DE368E CRC64;
MGKRRLTNTR LRVDFSKSQE ELDVPNLLML QKDSYDSFLY SNDSRESGIE RVLKSIFPIQ
DSAGRVTLEY AGCEFGKQKY TIAETMVRGL TYSIPLKIKI RLVLWDKDDK GEQVGVKDIK
EQTIYVREIP LMTDRVSFII NGVERVVVNQ LHRSPGVIFK EDESNTSANK LIYTGQIIPN
MGAWLYFEYD AKDIMYVRIN KRRKMPVTIL FRALGYSKQQ IIQMLYPVLD VSVKKDKFYI
PFNPNDIEGS LEYDLINEKG QVVLPAGKRF NKKRIRDLNE QNISYDKVEF STTNLLNTYL
AEPVIDSKSG EVILDTLSPL NEANIKKLND NKITKFKIIH DTAPGYDNSI INSFLADMES
LKNIRQTEKI DDECDLAAIR IYKVMRPAEP VTREVAHKFI EQLFFDPSRY DLTGVGRMKM
NHKLNLKVPD YVSVLTYEDI IETVKYLMQV RNGKGRIDDR DHLGNRRIRA IGELLANELH
SGLVKMQKSI KDKLTQQTSF ENVMPHDLIS SKMITSTIME FFASGQLSQF MDQTNPLSEI
THKRRLSALG EGGLVKERVG FEARDVHPTH YGRICPIETP EGQNIGLINT LSTFTKVNDL
GFIEAPYKKV VDGKTTNEVV YLTATQEDGK VIAPASTKLD STNKIVEGLI ETRCGGEISL
RKTEDVELID LSARMLVGVA ASLIPFLEHD DANRALMGSN MQRQAVPLLK PDAPIVGTGI
ESVIARDSWA AIKAKQGGVV EKVDGKNIYI LGENENGAYI DSYSMQKNMR TNQNTSFTQR
PIVKVGDKIK AGQIIADGAS MDSGELALGK NIRVAFMPWY GYNFEDAIVV SENIIKDDAF
TSVHIYEKEI EARELKHGIE EITADIPNVR EDSIAHLDES GIVKIGTYVT GGMILVGKVT
PKGDVKPTPE ERLLRAIFGE KAGHVVNKSL YCPQSMEGYV VDVKIFTKKG YEKDARARQA
YEDEKSDLDI EHHERLTMLN KEEMLRISYV LSKEPLSAEA KINDKVFKKG ECIPKKEFDD
INRFALNTLI KSYSKEIQNQ YEQIKNNFLE QKRVLGVEHE EKLAILEKDD ILPNGVVKLV
KIYIATKRKL KVGDKMAGRH GNKGIVSNIV PAVDMPYTKD GEPIDIILNP LGVPSRMNIG
QILEVHLGLI GKRFGEQIED ELKKSQYEFS TELKAKMIEI AKAVNEDDSV IKILESASKD
DLLAYARDWS NGVKFAIPVF EGISQEKFNK LFEMARIDMD GKTELYDGKT GEKIKERVNV
GYMYMLKLHH LVDEKVHARS TGPYSLVTQQ PVGGKALFGG QRFGEMEVWA LEAYGAAHTL
KEMLTIKSDD VNGRREAYEA ITKGYPIGDS AIPETFYVLT KELQSLALDV NVYGENQDEP
LVISEKEKDR PKDFSSFQIV LASPEKIRSW SRGEVKKPET INYRTLKPER DGLFCTKIFG
PVRDYECHCG KYRKGRYKDV ICEKCGVEVT TAKVRRSRMG HIELVTPVAH IWYVSSLPSR
IGTLLGVKMK DLERVLYYEA YIVKNAGDAY YDNELTKKVM KYDVLNEEQF KNLNGRFELA
GFEAQMGGEA VKELLEELDL VNLLESLKAD IAATNSEAKK KTYIKRLKVV ESFLQSGNRP
EWMMLSVLPV LPPDLRPLVA LDGGKFAVSD VNDLYRRVIN RNLRLKRLME LDAPEIIVRN
EKRMLQEAVD ALFDNGRNSN AVKGANKRPL KSLSEIIKGK QGRFRQNLLG KRVDFSGRSV
IVVGPNLRMD QCGLPKNMAI ELFKPHLLAK LEEKGHAKTI KTAKQMIDQK TNEVWECLQE
IIEGYPVMLN RAPTLHKQSI QAFHPKLIDG KAIQLHPLVC SAFNADFDGD QMAVHVPLSK
EAIAECKILM LSSANILLPA SGKPVAVPSQ DMVLGLYYLS LEKPDSKGEH KLFSNFNEIA
MAMEFDELDI HSTIRVVHER HVITTTAGRM VLRSILPSFV SPHLWNRVLK KKDISNLIDC
VYKESGIGGT AVFLDNLKDL GFKYATKAGI SIAAADIIIP DSKTKMITES KERVREIQSQ
AEQGALTIQE RYNKIIDVWT ETNDKMAKEM MEIVEKDRGG FNPIYMMADS GARGSATQIR
QLSAMRGLMA KPDGSIIETP IISNFKEGLN VLEYFTSTHG ARKGLADTAL KTANAGYLTR
KLIDVSQNVK ITMEDCGTHE GVELTDIAVG NEMIETLQER IVGRVTAAEV HDGISKEVLV
QEGKLITEEI AEQIKNAGVR AVNIRTPITC KAPRGICAKC YGLNLGEGKM SITGDSVGVI
AAQSIGEPGT QLTLRTFHVG GTASRSQEEN QIVANKEGFI RYYNIKTHKN REGKNIIANR
RNASVLLVEP KIKAPFDGEL QVETAHDRII LVLKGAKEQK TYELGKADIA AQRELAGVIG
EIEGKIYIPH DTGYKVKAGD SIADVIKDGW NVGNRIPYAS ELHIQDNEPV SQDIYANADG
VVKYYRLVSD ELERYHDVSV GMVVKEKGIF AVIADSNDRE ACRHYIARGS KIETKDNAEV
TKKTRIANKN NDKDAVVASW DAYNTLVIAE QAGTIRFNDV VAGTTVIEKE DEKTHIKSLT
VQEYIPQGYK PAIVVLDSKG KETTYNLEPK SVLLVNDGEK VEVADVLAKV PKATAKSKDI
TGGLPRVSEL FEARKPKDIA VLAEIDGHVS FGRAIRGKER VVITADDGRQ TEYLIDKSKQ
ILVREGEFVH AGEMLSDGTI SSHDILRING EKELHKYVVG EVQQVYRRQG VSIADKHIEV
ILSQMLRYFK VLDSGDTKFI EGDLVSRRHF KEENERMLKM GGNPAIAEPV LLGITRAAIS
SDSIISAASF QETTKVLTEA SISAKKDFLE DLKENVVLGR MIPVGTGLYK NKKVMIRHNK
DNS
//
