ID V6L8D2_HELPX Unreviewed; 2890 AA.
AC V6L8D2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=N871_03355 {ECO:0000313|EMBL:EST40665.1};
OS Helicobacter pylori X47-2AL.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1386083 {ECO:0000313|EMBL:EST40665.1, ECO:0000313|Proteomes:UP000017937};
RN [1] {ECO:0000313|EMBL:EST40665.1, ECO:0000313|Proteomes:UP000017937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X47-2AL {ECO:0000313|EMBL:EST40665.1,
RC ECO:0000313|Proteomes:UP000017937};
RX PubMed=24356847;
RA Veyrier F.J., Ecobichon C., Boneca I.G.;
RT "Draft Genome Sequence of Strain X47-2AL, a Feline Helicobacter pylori
RT Isolate.";
RL Genome Announc. 1:e01095-13(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:EST40665.1}.
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DR EMBL; AWNG01000010; EST40665.1; -; Genomic_DNA.
DR RefSeq; WP_023526455.1; NZ_AWNG01000010.1.
DR PATRIC; fig|1386083.3.peg.681; -.
DR Proteomes; UP000017937; 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; 1.
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; 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 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};
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 1624..1903
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
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 1451
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 1468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 1853
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2253
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"
FT BINDING 2263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2890 AA; 323659 MW; 36C5CDD483E250CC CRC64;
MSKKILLKNR LRADFTKTPT DLEVPNLLLL QRDSYDSFLY SKEGKESGIE 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 LGHDASIIQS FSADSESLKL
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 KANRTGVVEK IDSKNIYILG EGKEEAYIDA YSLQKNLRTN QNTSFNQVPI
VKVGDKVGAG 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 PIDIVLNPLG VPSRMNIGQI
LEMHLGLVGK EFGKQIARML ENKTKDFVKE LRAKMLEIAN AINEKDPLTI HALESCSDEE
LLEYAKDWSK GVKMAIPVFE GISQEKFYKL FELAKIAMDG KTDLYDGRTG EKMRERVNVG
YMYMIKLHHL VDEKVHARST GPYSLVTHQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
EMLTIKSDDI RGRENAYRAI AKGEQVGESE IPETFYVLTK ELQSLALDIN IFGDDVDEDG
VPKPIVIKED 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 NVKVVSDDCG THEGIEITDI AVGSELIEPL EERIFGRVLL EDVIDPITNE
ILLYADTLID EEGTKKVVEA GIKSITIRTP VTCKAPKGVC AKCYGLNLGE GKMSYPGEAV
GVVAAQSIGE PGTQLTLRTF HVGGTASRSQ DEREIVASKE GFVRFYNLRT YTNKEGKNII
ANRRNASILV VEPKIKAPFD GELRIETVYE EVVVSVKNSD QEAKFVLRRS DIVKPSELAG
VGGKIEGKVY LPYASGHKVH KGGSIADIIQ EGWNVPNRIP YASELLVKDN DPIAQDVYAK
EKGAIKYYVL EANHLERTHG IKKGDMVSEK GLFAVIADDN GREAARHYIA RGSEILIDDN
SEVSANSVIS KPTTNTFKTI ATWDPYNTPI IADFKGKVGF VDVIAGVTAA EKEDENTGIT
SLVVNDYIPS GYKPSLFLEG ANGEEVRYFL EPKTSIAISD GSSVEQAEVL AKIPKATVKS
RDITGGLPRV SELFEARKPK PKDVAILSEV DGIVSFGKPI RNKEHIIVTS KDGRSMDYFV
DKGKQILVHA DEFVHAGEAM TDGVVSSHDI LRISGEKELY KYIVSEVQQV YRRQGVSIAD
KHIEIIVSQM LRQVRILDSG DSKFIEGDLV SKKLFKEENA RMIALKCEPA IAEPVLLGIT
RAAIGSDSII SAASFQETTK VLTEASIAMK KDFLEDLKEN VVLGRMIPVG TGMYKNKKIV
LRTLEDGPKF
//
