(data stored in SCRATCH zone)

SWISSPROT: C8W3X7_DESAS

ID   C8W3X7_DESAS            Unreviewed;      1227 AA.
AC   C8W3X7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031, ECO:0000256|SAAS:SAAS01158594};
DE            Short=RNAP subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
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};
GN   Name=rpoB {ECO:0000256|HAMAP-Rule:MF_01321};
GN   OrderedLocusNames=Dtox_0278 {ECO:0000313|EMBL:ACV61231.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61231.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61231.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000256|HAMAP-Rule:MF_01321,
CC       ECO:0000256|RuleBase:RU363031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1
CC       beta' and 1 omega subunit. When a sigma factor is associated with
CC       the core the holoenzyme is formed, which can initiate
CC       transcription. {ECO:0000256|HAMAP-Rule:MF_01321,
CC       ECO:0000256|RuleBase:RU363031}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU000434}.
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DR   EMBL; CP001720; ACV61231.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0278; -.
DR   EnsemblBacteria; ACV61231; ACV61231; Dtox_0278.
DR   KEGG; dae:Dtox_0278; -.
DR   eggNOG; ENOG4108IIJ; Bacteria.
DR   eggNOG; COG0085; LUCA.
DR   HOGENOM; HOG000218612; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   BioCyc; DACE485916:G1GFV-293-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
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; -; 2.
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; 1.
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;
DR   PRODOM; C8W3X7.
DR   SWISS-2DPAGE; C8W3X7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031, ECO:0000313|EMBL:ACV61231.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031, ECO:0000313|EMBL:ACV61231.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031, ECO:0000313|EMBL:ACV61231.1}.
FT   DOMAIN       30    406       RNA_pol_Rpb2_1. {ECO:0000259|Pfam:
FT                                PF04563}.
FT   DOMAIN      141    281       RNA_pol_Rpb2_2. {ECO:0000259|Pfam:
FT                                PF04561}.
FT   DOMAIN      421    489       RNA_pol_Rpb2_3. {ECO:0000259|Pfam:
FT                                PF04565}.
FT   DOMAIN      499    566       RNA_pol_Rpb2_45. {ECO:0000259|Pfam:
FT                                PF10385}.
FT   DOMAIN      628   1013       RNA_pol_Rpb2_6. {ECO:0000259|Pfam:
FT                                PF00562}.
FT   DOMAIN     1015   1089       RNA_pol_Rpb2_7. {ECO:0000259|Pfam:
FT                                PF04560}.
SQ   SEQUENCE   1227 AA;  138507 MW;  2FA5F824FE39BF43 CRC64;
     MHWMVYAEKL GTRERLNFGK FKEVLDLPNL IEVQRNSYKW FLKNGLREVF HDISPIQDFT
     GNLVLEFLDY TLGEPKYFVE ECKERDVTYA APLRVKVRLI NKETGEVKEQ EVFMGDFPLM
     TEKGTFIING AERVIVSQLV RSPGVYFAEQ IDPSGKKLFS ATIIPNRGAW LEFETDVNDH
     VFVRIDRTRK IPATVLIRAL GYSSDAMVME EFGEDKNIQE TLSRDNTGSE EDALVEIYKR
     LRPGEPPTVE SARTLLETLF FDPKRYDLAN VGRYKLHKKL QHGVLYRYPE EQSGKIEYDE
     ILKQELPVER EFIRELTPKD ILDTIKYLLR LVQGITEEKD PLGRNIEYTV DDIDHLGNRR
     LRSVGELLQN QFRIGLSRME RVVRERMTIQ DVDVITPQVL INIRPVVASI KEFFGSSQLS
     QFMDQTNPLA ELTHKRRLSA LGPGGLSRER AGFEVRDVHH SHYGRMCPIE TPEGPNIGLI
     GSLSTYARIN QFGFIETPYR RVDKEKRIVT NEIEYLTADV EDRNIIAQAN APLNKEGFFT
     EQAVNARHGH EILKVPGEKI DFMDVSPKQV FSIATALIPF LEHDDANRAL MGANMQRQAV
     PLVKAQAPVV GTGVEYKAAR DSGVVPLARK SGIVEKVTAN DIMIRSDDGT SDYHKLLKFT
     RSNQGTCINQ RPIVTKGQRV DEGDIIADGP ATDNGELALG RNILVAFMPW DGYNYEDAIL
     ISEKAVKEDF FTSIHIEEYE CDARDTKLGP EEITRDIPNV GEEILKDLDD RGIIRVGAEV
     RPGDIMVGKV TPKGETELTA EERLLRAIFG EKAREVRDTS LRVPHGEAGK IVDVKVFSRD
     NGDELPPGVN HLVRVYIAQK RKISVGDKMA GRHGNKGVVA RIMPEEDMPF LPDGTPIEIV
     LNPLGVPSRM NIGQVLETHL GWAARKLGCY VSTPVFNGAT ESDILEFLRK ADLPDTAKTT
     LHDGRTGEPF DNPITVGYVY MLKLHHLVDD KIHARSTGPY SLVTQQPLGG KAQFGGQRFG
     EMEVWALEAY GSAYTLQEIL TVKSDDVVGR VKTYEAIVKG ENVPEPGVPE SFKVLIKELQ
     SLGLDVKVLS EDDREIEIKE IEEDIVETAK ELGIDLQDGG SKSTQKERID PPGCSIERVD
     DDLEDELEED DEEFNEDFLL QEVKLAQGGK LSEDIIDEPA DEEDFLDAED EDFADDIVGV
     KSKRLSNTDE WDEDLDYPDE DYDLDDE
//

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