RPOB_HISS2
ID RPOB_HISS2 Reviewed; 1342 AA.
AC B0URZ6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=HSM_0553;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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; CP000947; ACA32204.1; -; Genomic_DNA.
DR RefSeq; WP_012341386.1; NC_010519.1.
DR AlphaFoldDB; B0URZ6; -.
DR SMR; B0URZ6; -.
DR STRING; 228400.HSM_0553; -.
DR EnsemblBacteria; ACA32204; ACA32204; HSM_0553.
DR KEGG; hsm:HSM_0553; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 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; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086372"
SQ SEQUENCE 1342 AA; 149964 MW; C3627D10C0711916 CRC64;
MVYSYTEKKR IRKSFGKRPQ VLNVPYLLTI QLDSFDKFIQ RDPDGQQGLE AAFRSIFPIV
SNNGNTELQY VSYQLGEPVF DVRECQIRGT TYAASLRVKL RLVSYDKDAA SGTIKDIKEQ
EVYMGEIPLM TSNGTFVING TERVVVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLYARIDR RRKLPATIIL RALNYTTEEI LDLFFDKVSF EIKDNKLLMT
LVPERLRGET ASFDIEANGK VYIERGRRIT ARHIKALEKD KITQVEVPTE YIVGKVSAKD
YVDLTTGEII CPANMEISLE LLEKLSQAGY KNIETLFTND LDFGPYISET LRVDPSYDRL
SALVEIYRMM RPGEPPTKEA AEGLFDNLFF SSERYDLSAV GRMKFNRSLG IEDTTGSGTL
SKEDIVNVMR KLIDIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVKERLS
LGDLESVTPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HATHYGRVCP IETPEGPNIG LINSLSVYAR TNDYGFLETP YRKVVNGQVT
EEIEYLSAIE EGKYVIAQAN SNLDNELRFT DAFVTCRGEH GESGLYRPEE IHYMDVSTQQ
VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPVA LDSGVAVVAK
RGGTIQYVDA SRIVVKVNED ETIAGEAGID IYNLIKYTRS NQNTCINQIP CVQLGEPIER
GEILADGPST DLGELALGQN MRVAFMPWNG YNFEDSMLVS ERVVQEDRFT TIHIQELSCV
ARDTKLGSEE ITADIPNVGE AALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDGV EKDKRALEIE EMQLKQAKKD
LVEELEILEA GLFARVRNLL LSGGFNDKQL ENLDRTQWLE QTLVDEDKQN QLEQLAEQYE
ELRKDFEHKL EIKRSKIIQG DDLAPGVLKV VKVYLAVKRQ IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGQPVDIVLN PLGVPSRMNI GQILETHLGL AAKGIGDQIN AMIKQKQDVE
KLRGYIQKAY DLGDGSQKVD LSTFTDEEVL RLAKNLRKGM PLATPVFDGA HEKEIKALLE
LGGLPTSGQI ILFDGRTGEK FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVG GTHQMDPGTP
ESFNVIMKEI RSLGINIDLD EE
