ID T0F566_HELPX Unreviewed; 2502 AA.
AC T0F566;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU004279, ECO:0000256|RuleBase:RU363031};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE Flags: Fragment;
GN ORFNames=N207_07200 {ECO:0000313|EMBL:EPZ93221.1};
OS Helicobacter pylori UM114.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1355531 {ECO:0000313|EMBL:EPZ93221.1, ECO:0000313|Proteomes:UP000015605};
RN [1] {ECO:0000313|EMBL:EPZ93221.1, ECO:0000313|Proteomes:UP000015605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM114 {ECO:0000313|EMBL:EPZ93221.1,
RC ECO:0000313|Proteomes:UP000015605};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(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|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|RuleBase:RU004279};
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|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {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:EPZ93221.1}.
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DR EMBL; AUSS01000010; EPZ93221.1; -; Genomic_DNA.
DR RefSeq; WP_021309872.1; NZ_AUSS01000010.1.
DR Proteomes; UP000015605; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
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|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1624..1903
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT NON_TER 2502
FT /evidence="ECO:0000313|EMBL:EPZ93221.1"
SQ SEQUENCE 2502 AA; 281124 MW; 67DA924407702A9D CRC64;
MSKKIPLKNR LRADFTKTPT DLEVPNLLLL QRDSYDSFLY SKDGKESGIE KVFKSIFPIQ
DEHNRITLEY AGCEFGKSKY TVREAMERGI TYSIPLKIKV RLILWEKDTK SGEKNGIKDI
KEQSIFIREI PLMTERTSFI INGVERVVVN QLHRSPGVIF KEEESSTSLN KLIYTGQIIP
DRGSWLYFEY DSKDVLYARI NKRRKVPVTI LFRAMDYQKQ DIIKMFYPLV KVRYENDKYL
IPFASLDANQ RMEFDLKDPQ GKIILLAGKK LTSRKIKELK ENHLEWVEYP MDILLNRHLA
EPVMVGKEVL LDMLTQLDKN KLEKIHDLGV QEFVIINDLA LGHDASIIHS FSVDYESLKL
LKQTEKIDDE NALAAIRIHK VMKPGDPVTT EVAKQFVKKL FFDPERYDLT MVGRMKMNHK
LGLHVPDYIT TLTHEDIITT VKYLMKIKNN QGKIDDRDHL GNRRIRAVGE LLANELHSGL
VKMQKTIKDK LTTMSGAFDS LMPHDLVNSK MITSTIMEFF MGGQLSQFMD QTNPLSEVTH
KRRLSALGEG GLVKDRVGFE ARDVHPTHYG RICPIETPEG QNIGLINTLS TFTRVNDLGF
IEAPYKKVVD GKVVGETIYL TAIQEDSHII APASTPIDEE GNILGDLIET RVEGEIVLNE
KSKVTLMDLS SSMLVGVAAS LIPFLEHDDA NRALMGTNMQ RQAVPLLRSD APIVGTGIEK
IIARDSWGAI KANRAGVVEK IDSKNIYILG EGKEEAYIDA YSLQKNLRTN QNTSFNQVPI
VKVGDKVEAG QIIADGPSMD RGELALGKNV RVAFMPWNGY NFEDAIVVSE RITKDDIFTS
THIYEKEVDA RELKHGVEEF TADIPDVKEE ALAHLDESGI VKVGTYVSAG MILVGKTSPK
GEIKSTPEER LLRAIFGDKA GHVVNKSLYC PPSLEGTVID VKVFTKKGYE KDARVLSAYE
EEKAKLDMEH FDRLTMLNRE ELLRVSSLLS QAILEEPFSH NGKDYKEGDQ IPKEEIASIN
RFTLASLVKK YSKEVQNHYE ITKNNFLEQK KVLGEEHEEK LSILEKDDIL PNGVIKKVKL
YIATKRKLKV GDKMAGRHGN KGIVSNIVPV ADMPYTADGE PVDIVLNPLG VPSRMNIGQI
LEMHLGLVGK EFGKQIARML EDKTKGFAKE LHAKMLEIAN AINEKDPLTI HVLENCSDEE
LLEYAKDWSK GVKMAIPVFE GISQEKFYKL FELAKIAMDG KMDLYDGRTG EKMRERVNVG
YMYMIKLHHL VDEKVHARST GPYSLVTHQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
EMLTIKSDDI RGRENAYRAI AKGEQVGESE IPETFYVLTK ELQSLALDIN IFGDDVDEDG
APKPIVIKED DRPKDFSSFQ LTLASPEKIH SWSYGEVKKP ETINYRTLKP ERDGLFCMKI
FGPTKDYECL CGKYKKPRFK DIGTCEKCGV AITHSKVRRF RMGHIELATP VAHIWYVNSL
PSRIGTLLGV KMKDLERVLY YEAYIVKEPG EAAYDNEGTK LVMKYDILNE EQYQNISRRY
EDRGFVAQMG GEAIKDLLEE IDLITLLQSL KEEVKDTNSD AKKKKLIKRL KVVESFLNSG
NRPEWMMLTV LPVLPPDLRP LVALDGGKFA VSDVNELYRR VINRNQRLKR LMELGAPEII
VRNEKRMLQE AVDVLFDNGR STNAVKGANK RPLKSLSEII KGKQGRFRQN LLGKRVDFSG
RSVIVVGPNL KMDECGLPKN MALELFKPHL LSKLEERGYA TTLKQAKRMI EQKSNEVWEC
LQEITEGYPV LLNRAPTLHK QSIQAFHPKL IDGKAIQLHP LVCSAFNADF DGDQMAVHVP
LSQEAIAECK VLMLSSMNIL LPASGKAVAI PSQDMVLGLY YLSLEKSGVK GEHKLFSSVN
EIITAIDTKE LDIHAKIRVL DQGNIIATSA GRMIIKSILP DFIPTDLWNR PMKKKDIGVL
VDYVHKVGGI GITATFLDNL KTLGFRYATK AGISISMEDI ITPKDKQKMV EKAKVEVKKI
QQQYDQGLLT DQERYNKIID TWTEVNDKMS KEMMTAIAQD KEGFNSIYMM ADSGARGSAA
QIRQLSAMRG LMTKPDGSII ETPIISNFKE GLNVLEYFNS THGARKGLAD TALKTANAGY
LTRKLIDVSQ NVKVVSDNCG THEGIEITDI AVGSELIEPL EERIFGRVLL EDVIDPITNE
ILLYADTLID EEGAKKVVEA GIKSITIRTP VTCKAPKGVC AKCYGLNLGE GKMSYPGEAV
GVVAAQSIGE PGTQLTLRTF HVGGTASRSQ DEREIVASKE GFVRFYNLRT YTNKEGKNII
ANRRNASILV VEPKIKAPFD GELRIETVYE EVVVSVKNGE QEAKFVLRRS DIVKPSELAG
VGGKIEGKVY LPYASGHQVH KGGSIADIIQ EGWNVPNRIP YASELLVKDN DPIAQDVYAK
EKGAIKYYVL EVNHLERTHG IKKGDIVSEK GLFAVIADDN GR
//