ID T1CN96_9HELI Unreviewed; 2887 AA.
AC T1CN96;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=HFN_1862 {ECO:0000313|EMBL:GAD18264.1};
OS Helicobacter fennelliae MRY12-0050.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD18264.1, ECO:0000313|Proteomes:UP000018143};
RN [1] {ECO:0000313|EMBL:GAD18264.1, ECO:0000313|Proteomes:UP000018143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD18264.1,
RC ECO:0000313|Proteomes:UP000018143};
RA Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA Kuroda M., Shibayama K.;
RT "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT Isolated from a Bacteremia Patient.";
RL Genome Announc. 1:e00512-13(2013).
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:GAD18264.1}.
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DR EMBL; BASD01000004; GAD18264.1; -; Genomic_DNA.
DR RefSeq; WP_023946732.1; NZ_BASD01000004.1.
DR STRING; 1325130.HFN_1862; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000018143; 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:UP000018143};
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 1622..1901
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 1448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2887 AA; 323164 MW; 10F1277589773A2C CRC64;
MPNNKTKNRL RIDFTQQQNL DVPNLLLLQR DSYDTFLDAK DGKESGIEKV FKSIFPIQDA
QNRISLEYVG CEYGKPKYTI REAMERGITY AIPLKIKVQL IQWEKDEKGD KLAPKDIKEQ
TIFIREIPLM TDRTSFIING VERVVVNQLH RSPGVIFKQD ETNTANNKMI YMGQIIPDRG
SWLYFEYDSK DTLFVRINKR RKVPATILFR ALGYDKVDIL KIFYPILNIK IEKDKFLTRF
NPADFEGRVD FDIKDSKGEV IIASGKRLSA KKAKELKEKG LEWIEYPTET LVSRYLFEPI
IDKKSGEVIF DTLTQIDEAK LKKIAELKIK EIKIVNDLAT GLDSSIINSF IAETETIKQL
KQTEKIDNEN DLAAIRIYKV MRPGEPVTKE VAKQFVKRLF FEAESYDLTR VGRMKMNHKL
GLQIPNYITV LTLEDIIETT RYLIKVKNGE GRIDDRDNLG NRRIRAIGEL LANELHSGLV
KMQKAIKDKL TTMSGSFDAI MPHDLINAKM ITSTIIEFFT GGQLSQFMDQ TNPLSEITHK
RRLSALGEGG LVKERVGFEA RDVHPTHYGR ICPIETPEGQ NIGLINTIST FTLVNDLGFI
EAPYRKVVNG KVTDEIVYLT ATQEDGKVIA PASTQLDKDN KIIDSLIETR CGGEITLRKT
EDVELIDLSP RMLVGVAASL IPFLEHDDAN RALMGSNMQR QAVPLLKPDA PIVGTGMEQI
IARDSWEAIK ATRGGVVEKV DSKNIYILGE DEHGAYIDGY SLQKNLRTNQ NTCFAQHPIV
KQGEVVKAGQ IIADGASMDM GELALGKNIR VAFMPWNGYN FEDAIVVSEK LLKEDAFTSI
HIYEKEIIAR ELKHGTEEIT ADIPNVREEE VAHLDESGIV KIGTYVTAGM ILVGKVSPKG
EVKPTPEERL LRAIFGEKAG HVVNKSLYCP PSLEGTVIDV KIFTKKGYEK DARAISAYEK
EKSALDIEHH DRLTMLNKEE LLRVGLMLSK EELSADATIN NKTYKKGQKI PKEDIAGINR
FALNTLIKSY SKAVQAKYEK IKANFLEQKK TLGEEHEEKL QVLEKDDILP SGAVKQVKIY
IATKRKLKVG DKMAGRHGNK GIVSTIVPAV DMPYTIDGEP VDIVLNPLGV PSRMNIGQIL
EVHLGLVGKR FGEQIQDILE EQKGEFIKTL RSKMLSIAEL SNQKDSVIID LLKTCKDEEL
LHYARDWSKG VKFAIPVFEG ISQEKFNKLF EEAKIDMDGK VELYDGKTGE KIREKVNIGY
MYMLKLHHLV DEKVHARSTG PYSLVTQQPV GGKALFGGQR FGEMEVWALE AYGAAHTLKE
MLTIKSDDIV GRENAYRSIT KSEPVGESGI PETFFVLTKE LQSLTLDVNV FGDEVDEYGN
PKALEIKEDN RPKDFNSLQL VLASPENIRS WSKGEVKKPE TINYRTLKPE RDGLFCTKIF
GPVRDYECLC GKYKKPRYKG MVCEKCGVEV TTSKVRRSRI GHIELVTPVA HIWYVSSLPS
RIGTLLGVKM KDLERVLYYE AYIVKEAGEA FYDNESTKPV MKYDVLNEEQ YQNIQQRFGD
KGFVAQMGGE AVKELLEQLD LTALFQALRE EIKSTNSESK KKSIVKRLKV VENFLNSGNR
PEWMMLTVLP VLPPDLRPLV ALDGGKFAVS DVNDLYRRVI NRNQRLKRLL ELDAPEIIVR
NEKRMLQEAV DALFDNGRNA NAVKGANKRP LKSLSEIIKG KQGRFRQNLL GKRVDFSGRS
VIVVGPNLRM DQCGLPKNMA LELFKPHLLA KLEEKGYAST LKQAKKMIEQ KTNEVWECLQ
EIVEGYPVLL NRAPTLHKQS IQAFHPKLID GKAIQLHPLV CSAFNADFDG DQMAVHVPLS
QEAITECKVL MLSSMNILLP ASGKAVAVPS QDIVLGLYYL SLEKKGVKGE HKLFGDIHQI
MIAIETGNLD INAKIRTLVD GRIITTTAGR MILHSILPTQ VPINLWNKVL KKKDISTLTD
YVYKEAGNGI TATFLDNLKN LGFRYATKAG ISISAADIII PENKNEIIKK ANKETRNIRD
MFESGSITEE ERYNKTIDIW TEAGNELSKV MMKLIEADKG GFNSIYMMAD SGARGSAAQI
RQLSAMRGLM AKPDGTIIET PIISNFKEGL NALEYFTSTH GARKGLADTA LKTANAGYLT
RKLIDVSQNV KISIEDCGTH EGVEISDIIE GSELIESLEE RVFGRVLATD VIDPITNEIL
FSAETLIDEK AAKRIIEANV KSVIIRTPVT CKALKGVCAK CYGLNLGEGK MVRPGEAVGV
IAAQSIGEPG TQLTLRTFHV GGTASRTQEE KEIRAEKEGF IRYYNLKTYT NKEGKNIITN
RRNAAVLVVE PKIKAPFDGV LHIETAHDEI IISIKGAKQE VKYSVRKSDV AKPNELAGVS
GRLEGKLYIA HESGYKVSEG GSIVDVVKDG WNVPNRIPYA SEIIAKDNAP ISQTITAKEK
GIVKFYFLES DHLQRVHDIK VGDVIEEKGI FAVIADENDR EATRHYIARE SKILVDDNSA
VEIDTIIAEP TNKANNLIAT WDPYNTPVIS DIDGVVHFKD IIPGLTVAEQ EDEMSGIRSL
MVNDYIPSGY QPSILIEGKK ETKQYLLEPN TSIAVTEGMN VALADILAKT PKATVKSRDI
TGGLPRISEL FEARKPREVA ILSEIDGIVS FGKAIRGKER VIITGKDGSI SEYLIDRTKR
ILVHKDEFVH AGEAITDGIT SSHDILRIGG EKELLRFIVN EVQQVYRGQG VTIADKHIEV
IVSQMLRQVR IIDPGNTKFV ENDLVSKRHF KEENERIMQL GGEPAIADLA LLGITRAAIS
SDSIISAASF QETTKVLTEA SIAAKKDFLE DLKENVVLGR MIPVGTGLYK NKRFVIKPKI
LDLMHKI
//
