ID A0A4U8UGH5_9HELI Unreviewed; 2885 AA.
AC A0A4U8UGH5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=LS72_002200 {ECO:0000313|EMBL:TLE16723.1};
OS Helicobacter apodemus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=135569 {ECO:0000313|EMBL:TLE16723.1, ECO:0000313|Proteomes:UP000029920};
RN [1] {ECO:0000313|EMBL:TLE16723.1, ECO:0000313|Proteomes:UP000029920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT-03-7007 {ECO:0000313|EMBL:TLE16723.1,
RC ECO:0000313|Proteomes:UP000029920};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(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:TLE16723.1}.
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DR EMBL; JRPC02000004; TLE16723.1; -; Genomic_DNA.
DR Proteomes; UP000029920; 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; 1.
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:UP000029920};
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 1625..1904
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 1464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 1852
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1854
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 2254
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"
FT BINDING 2264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2885 AA; 323343 MW; 81405BBC6DF1D3F1 CRC64;
MIMPVSLKSG NRLRVDFTKI PQNIAVPNLL QLQRNSYDAF LKAQEAGDSG IEKVFKSIFP
IHDTQNRISL EYAGCEYGKP RYTVREAMER GLTYSIPLKI KIRLVLWERD EKTGEKLGVK
DIKEQSIFVR EIPLMTERTS FIINGVERVV VNQLHRSPGV IFKEEESSSA SNKLVYTGQI
IPDRGSWLYF EYDVKDTLFV RVNKRRKVPV TILFRALGYS KQDILKMFYP LLEIKSKNGK
YFIPFNPEEF IGRVEFDIKD AKGNLIVAAG KRLTAKKAKT LQEEKLNMIE YPNDILMNRY
LAEPILDKES GEILFDTLTL LDESKLKKLQ ELNINHFIIA NDLAAGVDAS IINSFIADAE
SLKLLKQTEK IDNENDLAMI RIYKVMRPGE PVTKDVAKQF IQQLFFDPER YDLTPVGRMK
MNHKLDINVP DYVTVLTYED IIKTVRYLMH VKNGQGRIDD RDHLGNRRIR AIGELLANEL
HTGLVKMQKA IRDKLSTISS GLEELMPHDL VNSKMITSTI LEFFTGGQLS QFMDQTNPLS
EVTHKRRLSA LGEGGLVKER AGFEVRDVHP THYGRICPIE TPEGQNIGLI NTLSTYAKVN
ELGFIEAPYR KVVNRKVTNE IVYLTATQEE GAVIAPASTI LASDDSIKED IIEVRKDGEI
ILMESSKVDL IDLSPRMVVG VAASLIPFLE HDDANRALMG SNMQRQAVPL LAPEAPVVGT
GIEKIVSRDS WEAIKAKRDG VVEKVDSKNI YILGEDDSGA FIDHYSLQKN LRTNQNTCFS
QKPIIKAGDV IKAGDVIADG PNMDQGELAL GKNIRVAFMP WNGYNFEDAI VVSEKLICND
TFTSIHIYEK EIEARELKHG VEEITRDIPN IREEELSHLD ESGIVRIGTY VSGGMILVGK
VSPKGEVKPT PEERLLRAIF GEKAGHVVNK SLYCPPSLEG TVIDVKIFTK KGYDKDKRAI
VAYEEEKARL DLEHHDKLLM LDREENLRIS SILSKEKLTS NAKIADKEYK KGSVIPKKEL
ESVNRFAMAT LIKSYSKDIQ SKYEALKGNF LEQKKNLSQE HEEKLSIIEK DDILPSGVVK
LVKIYVATKR KLKVGDKMAG RHGNKGIVSN IVPEMDMPYT EDGRPVEIVL NPLGVPSRMN
IGQILEVHLG LVGKQLGEQI ASVFEIEKSK WITTLRERIK EIVKHSNMQI SKAFLENLSD
EELIAYARDW SKGVKFATPI FEGVNAQEFE KLFELAKIDT DGKTELYDGR TGEKMIERVN
VGYMYMLKLH HLVDEKVHAR STGPYSLVTQ QPVGGKALFG GQRFGEMEVW ALEAYGAAHT
LKEMLTIKSD DVEGRVKAYK AITRGEAVKE SEIPETFYVL TKELQSLALD VNVFVKNKEG
INESITIKEE DRPSDFNAFQ LLLASPEKIR SWSNGEVKKP ETINYRTLKP ERDGLFCAKI
FGPTRDYECL CGKYKKMRYK GVICEKCGVE VTSSKVRRSR MGHIELVTPV AHIWYVNSLP
SRIGTLLGVK MKDLERVLYY EAYIVKQPGE AYYDNESTKP VTKYDVLNEE QYQSLSQRFE
HTGFIAQMGG EAVKELLEGL DLVDLIGELK EAIKATNSEA KKKTIIKRLK IVESFVISGE
QNRPEWMMLT VLPVLPPDLR PLVALDGGKF AVSDVNDLYR RVINRNQRLK RLIELDAPEI
IVRNEKRMLQ EAVDALFDNG RNANAVKGAN KRPLKSLSEI IKGKQGRFRQ NLLGKRVDFS
GRSVIVVGPN LRMDECGLPK GMALELFRPH ILAKLEEKGY ATTLKQAKKM IEQKSNEVWE
CLQEIVANYP IMLNRAPTLH KQSIQAFHPK LIDGKAIQLH PLVCAAFNAD FDGDQMAVHV
PLSQEAITEC KLLMLSSMNI LLPASGKAVT VPSQDMVLGL YYLSLEKNSS KGEHKLFSDI
DQILVALEND VVEIGSKVRV LVEDKIINTT IGRMILKSIL PEFVPTHLWN KVLKKKDIAT
LIDYVYKEGG VGITASFLDD LKNLGFKYAT KAGISISADD IIVPNNKNKV VEGAKKKVKD
IQAQFSAGLL TEQERYNKII DVWTDTNNAL GNEMMKLIEE DKSGFNSIYM MADSGARGSA
GQIRQLSAMR GLMAKPDGTI IETPITSNFK EGLNVLEYFI STHGARKGLA DTALKTANAG
YLTRKLIDVS QNVKVVMHDC GTNEGIEITD ITVGSELIEP LEERIFGRII AENIIDPITN
EVLISEGVMI DEEKARKIKE AGVKSVIIRT PVTCKAEKGV CAKCYGLNLG ESRISKVGEA
VGVVAAQSIG EPGTQLTLRT FHIGGTASRS QEERQVIADK EGFIRYYNVK TYKNREGRII
VSNRRNAAIL LVEPKIKAPF EGELKIDVVH DEVIVSVVGK NETAKFVLRK SDVAKPNELA
GVTGKIEGKF YIPYVNGHYV RDGGSIVDII KDSWNIPNRI SYASELKVED NAPITQKIYA
KESGIVKYYY LQGDHLERYR ALKKGEKITE KGLFAVIADE YEQEAARHYI ARDSIIEVED
NQRVDKGMLI AKPISDEHIV IADWDPYSNP IISEEAGIIK FEDIIPGLTV SEQTDELTGQ
TRLVVNEYIS SAYKPTLVLS TDTGGLIRYT LDPKTAIFVK DGAKVEMADI LAKTPKALVK
SKDITGGLPR VSELFEARKP KEPAILAEID GVVSFGKPIR GKEKIVVTAN DGRIAEYLID
KSKQILVHEG EFVHAGEAIT DGVIASQDIL RIGGEKELYK YIVSEVQQVY RRQGVSIADK
HIEIIVSQML RQVRIYDSGN TKFIEGDLVS KRHFKEENMR IIKMGGIPAI AEPVLLGITR
AAIGSDSVIS AASFQETTKV LTEASIAAKI DNLEDLKENI VLGRMIPVGT GIYKEMKIKV
KENLP
//
