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RPOBC_HELPH
ID   RPOBC_HELPH             Reviewed;        2890 AA.
AC   Q1CS68;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Bifunctional DNA-directed RNA polymerase subunit beta-beta';
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322};
DE   Includes:
DE     RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE     AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE     AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   Includes:
DE     RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE     AltName: Full=RNA polymerase beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE     AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoBC; OrderedLocusNames=HPAG1_1137;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322}.
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:0000255|HAMAP-Rule:MF_01321,
CC         ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta/beta' and
CC       1 omega subunit. When a sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- MISCELLANEOUS: Fusion of rpoB and rpoC occurs naturally in Helicobacter
CC       species and at least some Wolbachia; the protein has been artificially
CC       split in two in H.pylori. The split protein seems to function normally.
CC       {ECO:0000250|UniProtKB:O25806}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the RNA polymerase
CC       beta chain family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the RNA polymerase
CC       beta' chain family. {ECO:0000305}.
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DR   EMBL; CP000241; ABF85204.1; -; Genomic_DNA.
DR   RefSeq; WP_000037890.1; NC_008086.1.
DR   SMR; Q1CS68; -.
DR   PRIDE; Q1CS68; -.
DR   EnsemblBacteria; ABF85204; ABF85204; HPAG1_1137.
DR   KEGG; hpa:HPAG1_1137; -.
DR   HOGENOM; CLU_000524_0_0_7; -.
DR   OMA; QTEKIDD; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000008835; Chromosome.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
DR   Gene3D; 4.10.860.120; -; 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   PANTHER; PTHR19376; PTHR19376; 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   TIGRFAMs; TIGR02013; rpoB; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..2890
FT                   /note="Bifunctional DNA-directed RNA polymerase subunit
FT                   beta-beta'"
FT                   /id="PRO_0000300130"
FT   REGION          1..1377
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT   REGION          1384..2890
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT   BINDING         1449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1451
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1465
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1468
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1849
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1851
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1853
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         2179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         2253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         2260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         2263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   2890 AA;  323863 MW;  C9B9613666846C8B CRC64;
     MSKKIPLKNR LRADFTKTPT DLEVPNLLSL QRDSYDSFLY SKDGKESGIE KVFKSIFPIQ
     DEHNRITLEY AGCEFGKSKY TVREAMERGI TYSIPLKIKV RLILWEKDTK SGEKNGIKDI
     KEQSIFIREI PLMTERTSFI INGVERVVVN QLHRSPGVIF KEEESSTSLN KLIYTGQIIP
     DRGSWLYFEY DSKDVLYARI NKRRKVPVTI LFRAMDYQKQ DIIKMFYPLV KVRYENDKYL
     IPFASLDANQ RMEFDLKDSQ GKIILLAGKK LTSKKIKELK ENHLEWVEYP MDILINRHLA
     EPVMVGKEVL LDMLTQLDKN KLEKIHDLGV QEFVIINDLA LGHDASIIHS FLADYESLRL
     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 KANRAGAVEK 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 EDKTKDFAKE LRVKMLEIAN AINEKDPLTI HALENCSDEE
     LLEYAKDWSK GVKMAIPVFE GISQEKFYKL FELAKIAMDG KMDLYDGRTG EKMRERVNVG
     YMYMIKLHHL VDEKVHARST GPYSLVTHQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
     EMLTIKSDDI RGRENAYRAI VKGEQVGESE IPETFYVLTK ELQSLALDIN IFGDDVDEDG
     APKPIVIKED DRPKDFSSFQ LTLASPEKIH SWSYGEVKKP ETINYRTLKP ERDGLFCMKI
     FGPTKDYECL CGKYKKPRFK DIGTCEKCGV AITHSKVRRF RMGHIELATP VAHIWYVNSL
     PSRISTLLGV KMKDLERVLY YEAYIVKEPG EAAYDNEGTK LVMKYDILNE EQYQNISRRY
     EDRGFIAQMG 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 KEMMIAIAKD KEGFNSIYMM ADSGARGSAA
     QIRQLSAMRG LMTKPDGSII ETPIISNFKE GLNVLEYFNS THGARKGLAD TALKTANAGY
     LTRKLIDVSQ NVKVVSDDCG THEGIEITDI AVGSELIEPL EERIFGRVLL EDVIDPITNE
     ILLYADTLID EEGAKKVVEA GIKSITIRTP VTCKAPKGVC AKCYGLNLGE GKMSYPGEAV
     GVVAAQSIGE PGTQLTLRTF HVGGTASRSQ DEREIVASKE GFVRFYNLRT YTNKEGKNII
     ANRRNASILV VEPKIKAPFD GELRIETVYE EVVVSVKNGE QEAKFVLRRS DIVKPSELAG
     VGGKIEGKVY LPYASGHKVH KGGSIADIIQ EGWNVPNRIP YASELLVKDN DPIAQDVYAK
     EKGTIKYYVL EANHLERTHG IKKGDMVSEK GLFAVVADDN GREAARHYIA RGSEILIDDN
     SEVSANSVIS KLTTNTFKTI ATWDPYNTPI IADFKGKVSF VDVIAGVTVA EKEDENTGIT
     SLVVNDYIPS GYKPSLFLEG ANGEEMRYFL EPKTSIAISD GSSVEQAEVL AKIPKATVKS
     RDITGGLPRV SELFEARKPK PKDVAILSEV DGIVSFGKPI RNKEHIIVTS KDGRSMDYFV
     DKGKQILVHA DEFVHAGEAM TDGVISSHDI LRISGEKELY KYIVSEVQQV YRRQGVSIAD
     KHIEIIVSQM LRQVRILDSG DSKFIEGDLV SKKLFKEENA RMIALKGEPA IAEPVLLGIT
     RAAIGSDSII SAASFQETTK VLTEASIAMK KDFLEDLKEN VVLGRMIPVG TGMYKNKKIV
     LRTLEDGPKF
 
 
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