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RPOB_PHEZH
ID   RPOB_PHEZH              Reviewed;        1356 AA.
AC   B4R8K5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {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};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=PHZ_c1218;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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}.
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   -!- 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:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; CP000747; ACG77632.1; -; Genomic_DNA.
DR   RefSeq; WP_012521777.1; NC_011144.1.
DR   AlphaFoldDB; B4R8K5; -.
DR   SMR; B4R8K5; -.
DR   STRING; 450851.PHZ_c1218; -.
DR   PRIDE; B4R8K5; -.
DR   EnsemblBacteria; ACG77632; ACG77632; PHZ_c1218.
DR   KEGG; pzu:PHZ_c1218; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_5; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001868; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 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; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
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   PANTHER; PTHR20856; PTHR20856; 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   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1356
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141716"
SQ   SEQUENCE   1356 AA;  151282 MW;  4EDABC4BCFEBA45B CRC64;
     MAQSFTGKKR IRKSFGRIPE AVQMPNLIEV QRSSYEQFLQ REVRAGERRD EGIEAVFKSV
     FPIKDFNERA VLEYVSYEFE EPKYDVEECV QRDMTYAAPL KVKLRLIVFE TDEETGARSV
     KDIKEQDVYM GDIPLMTEKG TFIVNGTQRV IVSQMHRSPG VFFDHDKGKT HASGKLLFAA
     RVIPYRGSWL DFEFDAKDIV YVRIDRRRKL PATTFLMALG MDGEEILSTF YETVPYEKKG
     DGWATPYKPE RWRGVKPEFP LIDADTGEEI APAGQKISAR NAKKFADNGL KTLLLAPEAL
     TGRYLAKDLV NFETGEIYAE AGDELDPTLL AALEEQGFTT LDVLDIDEVT VGAYIRNTLR
     VDKNTAREDA LFDIYRVMRP GEPPTVEAAE AMFKSLFFDS ERYDLSSVGR VKMNMRLELD
     CPDDVRVIRK EDVIAVLLTL VGLRDGRGEI DDIDNLGNRR VRSVGELLEN QYRVGLLRME
     RAIKERMSSV DIDTVMPHDL INAKPAAAAV REFFGSSQLS QFMDQTNPLS EITHKRRLSA
     LGPGGLTRER AGFEVRDVHP THYGRICPIE TPEGPNIGLI NSLATHAVVN KYGFIESPYR
     RIRDGKTTDE VVYMSAMEEA KHVIAQANIK LENGEIVEDL VPGRINGEPS LLPKADVDLM
     DVSPKQVVSV AASLIPFLEN DDANRALMGS NMQKQAVPLI QSDAPLVGTG MESIVAVDSG
     AVVVARRTGV VEQIDGTRIV VRATEETDPS KPGVDIYRLQ KFQRSNTSTC INQRPLVRVG
     DKINAGDVIA DGPSTELGEL ALGRNALVAF MPWNGYNFED SILISERIVR DDVFTSIHIE
     EFEVMARDTK LGPEEITRDI PNVGEEALRN LDEAGIVAIG AEVQPGDILV GKVTPKGESP
     MTPEEKLLRA IFGEKASDVR DTSLRLPPGV SGTIVEVRVF NRHGVDKDER ALAIERAEID
     RLGKDRDDEF AILNRNMQGR LRQLLVGKTA VSGPKGLGRG EITAEKLEEI APGLWWQIAL
     DDEKAMGELE ALRKQFDDAR KRLDRRFEDK VDKLQRGDEL PPGVMKMVKV FVAVKRKLQP
     GDKMAGRHGN KGVISKILPI EDMPYLEDGT SVDIVLNPLG VPSRMNVGQI FETHLGWAAA
     GLGKQVQRLL EDWQHGGQKQ ALIEHLRDVY GPDEELPDTE EELVELARNL SKGIPFATPV
     FDGAHIDDIE NLLEKAGLDR SGQSYLYDGQ SGERFKRPVT VGYIYMLKLH HLVDDKIHAR
     SIGPYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT LQEMLTVKSD DVAGRTKVYE
     SIVRGDDTFE AGIPESFNVL VKEMRSLGLN VELENS
 
 
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