(data stored in ACNUC7421 zone)

SWISSPROT: RPOB_ALCBS

ID   RPOB_ALCBS              Reviewed;        1380 AA.
AC   Q0VSM2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 87.
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=ABO_0378;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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}.
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, ChEBI:CHEBI:83400;
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}.
DR   EMBL; AM286690; CAL15826.1; -; Genomic_DNA.
DR   RefSeq; WP_011587673.1; NC_008260.1.
DR   SMR; Q0VSM2; -.
DR   STRING; 393595.ABO_0378; -.
DR   PRIDE; Q0VSM2; -.
DR   EnsemblBacteria; CAL15826; CAL15826; ABO_0378.
DR   KEGG; abo:ABO_0378; -.
DR   eggNOG; ENOG4108IIJ; Bacteria.
DR   eggNOG; COG0085; LUCA.
DR   HOGENOM; HOG000218612; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   BioCyc; ABOR393595:ABO_RS01975-MONOMER; -.
DR   Proteomes; UP000008871; 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; 2.40.270.10; -; 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; 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;
DR   PRODOM; Q0VSM2.
DR   SWISS-2DPAGE; Q0VSM2.
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1380
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300275"
SQ   SEQUENCE   1380 AA;  154611 MW;  93928BB33230066D CRC64;
     MAYSFTEKKR IRKDFGKLPK VMEVPYLLAI QLDSYRKFLQ QDKSAEERLE EGLEAAFRSV
     FPIASYSGNA ALEYAGYEFG KPVFDVKECI IRGTTYAAPL RVRIRLVIYD RESSGAIKDI
     REQQVYMGEI PLMTENGTFV INGTERVIVS QLHRSPGVFF DHDKGKTHSS GKLLYSARVI
     PYRGSWLDFE FDPKDQVFVR IDRRRKLPAT ILLRALGYTS DEVLEMFFDT NEIAVEDGIY
     RMKLVPERLR GETATFDILA DGEVVVERGR RITARHIRQL EKANIEYLDI PAEYLQGKYL
     AKSIIDQDTG EILVECNTEL TAETLEKLEQ GGITDFETLY TNDLDNGPFM ADTLRADPTR
     TPLEALVEIY RMMRPGEPPT KEAAENLFKN LFFTDERYDL STVGRMKFNR RLGREDETGP
     GILYDGRYFS ARSDEEGKQY FEQMGGETSD IIDVLRTLVD IRNGNGVVDD IDHLGNRRVR
     SVGEMAENQF RVGLVRVERA VKERLSLAES EGLMPQDLIN SKPVAAAVKE FFGSSQLSQF
     MDQNNPLSEI THKRRVSALG PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS
     LATYARANEY GFLESPYLKV IDGKVSEEIE YLSAIEEAEC VIAQVDAKMT EEGGFEEDFV
     TVRHRYEFTV MERDTITHMD VSPRQVVSVA ASLIPFLEHD DANRALMGSN MQRQAVPTLR
     ADKPLVGTGF ERHVARDSGV CVVATRGGIV DKVDASRIIV KVNDDEVSEG EAGVDIYNLT
     KYTRSNQNTC INQRPLVKVG DRVAARDIMA DGPSVDMGEL ALGQNMRVAF MPWNGYNFED
     SILISEKVVK DDRFTSIHIQ ELTCIARDTK LGPEEITADI PNVGEAALSK LDESGIVYIG
     AEVEAGDILV GKVTPKGETQ LTPEEKLLRA IFGEKASDVK DTSQRVSSGV KGTIIDVQVF
     TRDGVEKDER ARQIEQAALE QFRKDLKDEY RILELDILER LRAVMVGKKV NGGAGFKRGT
     EMTGEILDGL DAEKWFELRP ADDDVAEQLE RAQQYLEQHK KEQDERYKDK QAKISGGDDL
     AHGVLKVVKV YLAIKRRIQP GDKMAGRHGN KGVISVIMPE EDMPHDENGV PVDVVLNPLG
     VPSRMNVGQI LETHLGWAAK GLGERIGEML AEQKKIADIR VFLDKIYNQA GAGGTPEDLD
     SFSDDEIIEL AKNLVGGVPM ATAVFDGAKE FEIKELLELA GHDRSGQVQL WDGRTGEAFD
     RKVTVGYMYM LKLNHLVDDK MHARSTGSYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG
     AAYTLQEMLT VKSDDVNGRT RVYKNIVDGD HRMDPGMPES FNVLLKEIRS LGINIELEND
//

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