RPOB_CAMFF
ID RPOB_CAMFF Reviewed; 1379 AA.
AC A0RQI5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, 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};
GN OrderedLocusNames=CFF8240_1316;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK83065.1; -; Genomic_DNA.
DR RefSeq; WP_011732163.1; NC_008599.1.
DR AlphaFoldDB; A0RQI5; -.
DR SMR; A0RQI5; -.
DR STRING; 360106.CFF8240_1316; -.
DR PRIDE; A0RQI5; -.
DR EnsemblBacteria; ABK83065; ABK83065; CFF8240_1316.
DR GeneID; 61065134; -.
DR KEGG; cff:CFF8240_1316; -.
DR PATRIC; fig|360106.6.peg.1286; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000760; 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; Transcription;
KW Transferase.
FT CHAIN 1..1379
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300294"
SQ SEQUENCE 1379 AA; 156299 MW; 57F5429903859F20 CRC64;
MLNSLYSGNR LRVDFSNVAK EIDVPNLLQL QKKSFDHFLN LDNSQTESGI EKVFKSIFPI
HDPQNRLTLE YVSSEISKPR YTVRECMERG LTYCVNLKIK IRLIVHDRDE KTSEKVGVKD
IKEQEIFVRE IPLMTDRISF IINGVERVVV NQLHRSPGVI FKEEESPTVV NKLIYTAQII
PDRGSWLYFE YDTKDVLYVR INKRRKVPIT ILFRALGYKK QDIVKLFYPI QTLNIKNNKF
LTMFNPDDFS GRVDYDIKDE DGNILHQAGK RLTKKKADKL IEDGLKFVEY PIEVLVNRYL
ASPVIDKESG EVIYDTLTQL DENKLAKIVA EQNSIEIAND LASGVDDAII NSFLQDYETL
KLLKQTEGLE DENDLAAIRI YKVMRPGEPV VKEAARTFVN DLFFNPERYD LTKVGRMKMN
HKLGLSVPEY VTVLTNEDII KTAKYLIKVK NGQGYIDDRD HLGNRRIRSI GELLANELHL
GFVKMQKAIR DKFTSLSNNV DELMPYDLVN PKMITTTIME FFTGGQLSQF MDQTNPLSEV
THKRRLSALG EGGLVKERAG FEVRDVHPTH YGRICPVETP EGQNIGLINT LSTYAKVNDL
GFVESPYRRV IDGKVTNEIV YLTATQEEGH IIAPASTVLD ANDIIKEDLI EVRRDGEMLL
AKREDVTLID LCSGMVMGVA ASLIPFLEHD DANRALMGSN MQRQAVPLLR STAPIVGTGM
EAIVARDAWE AIKAKRGGVI EKVDNRNIFI LGEDENGPYI DQYTMEKNLR TNQNTTFSQH
PIVKKGDMVK SGQIIADGSS MEKGELAIGK NALIAFMPWN GYNYEDAIVM SERMIRADAF
TSVHIYEKEI EARELKDGVE EITRDIPNMK EEDLMHLDES GIVKIGTHIK PGMILVGKVS
PKGEVKPTPE ERLLRAIFGE KAGHVVNKSL YAGASLEGVV IDVKIFTKKG YEKDARSFKA
YEDEKNILEK EHHDRLLMLD REEMLRVTAL LSKNPLESEL EIGKNSYKKG DKIKRSDLDN
VNRFTLNTYV KCFSKEIQKT YEDMKAYFQN EKKKLKDEHD AKLEILEKDD ILPSGVVKLV
KVYLATKRKL KVGDKMAGRH GNKGIVSNIV PDVDMPYLPN GRTVDIVLNP LGVPSRMNIG
QILESHLGLV GMKLGEQIEE IFENKKAEWI KELRAKMTEI ADVSRLMDAK AILSKIDDDK
LIDYARDWAS GVRFATPIFE GVKADEFKKL FEMAKIDMDG KTELYDGRTG SKMAERVNVG
CMYMLKLHHL VDEKVHARST GPYSLVTQQP VGGKALSGGQ RFGEMEVWAL EAYGAAHTLR
EMLTVKSDDV EGRLAAYKAL TRGENVPSTG IPETFFVLTN ELKSLALDVE IYDEEENNE
