RPOB_GLAP5
ID RPOB_GLAP5 Reviewed; 1342 AA.
AC B8F741;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=HAPS_1592;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL33143.1; -; Genomic_DNA.
DR RefSeq; WP_010787245.1; NC_011852.1.
DR AlphaFoldDB; B8F741; -.
DR SMR; B8F741; -.
DR STRING; 557723.HAPS_1592; -.
DR PRIDE; B8F741; -.
DR EnsemblBacteria; ACL33143; ACL33143; HAPS_1592.
DR GeneID; 66617752; -.
DR KEGG; hap:HAPS_1592; -.
DR PATRIC; fig|557723.8.peg.1562; -.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006743; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165809"
SQ SEQUENCE 1342 AA; 149537 MW; 0A06A7E92842DE12 CRC64;
MAYSYSEKKR IRKSFGKRSQ VLNVPYLLTI QLDSFDKFIQ RDPEGLQGLE AAFRSVFPIV
SSNGATELQY VSYELGEPVF DVRECQIRGT TYAAPLRVKL RLVTFDREAA AGTVKDIKEQ
NVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHASGKV LYNARIIPYR
GSWLDFEFDP KDNLYARIDR RRKLPATIIL RALGYTTEEI LNMFFETATF HIEDNRLLMT
LVPERLRGET AAFDIEANGK IYVESGRRIT ARHIRALEKD NITQIQVPTE YIVGRVTARD
YVDLSTGEIV CPANSEIGLE TLAALAQAGY NEIEVLFTND LDYGPYISET LRIDPTYDRL
SALVEIYRMM RPGEPPTKEA AEALFDNMFF STDRYDLSAV GRMKFNRSLD IPEGVGTGIL
SNDDIIGVMK KLIEIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVRERLS
LGDLDGVTPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGSGGLTR
ERAGFEVRDV HTTHYGRLCP IETPEGPNIG LINSLSVYAR TNNYGFLETP FRKVVNGQVT
EEIEYLSAIE EGAYVIAQAN SNLDENFRFT DTYVTCRGEH GESGLYRPEE IHYMDVSTQQ
VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAVIAK
RGGTIQYVDA SRIVVKVNED ETVAGEAGID IYNLIKYTRS NQNTCINQIP CVKLGEPVGR
GEILADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQEDRFT TIHIQELSCV
ARDTKLGAEE ITADIPNVGE SALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLIPEE
KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDGV EKDKRAKDIE EIQLREAKKD
LTEELEILEA GLFTRVRNLL LEGGVAQATL DNLAREKWLE QTLDDEAKQN QLEQLAEQHE
ELRKEFERKL EIKRNKIIQG DDLAPGVLKV VKVYLAVKRQ IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGQPVEIVLN PLGVPSRMNI GQILETHLGL AARGIGDQID KMIKQQQEIA
KLREYIQKAY DLGHGAQSVD LSTFSDEEVM RLAQNLRKGL PLATPVFDGA HESEIKGLLE
LGGLPTSGQI TLYDGRTGEK FERLVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQLGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GTHYMEPGIP
ESFNVITKEI RALAIDMELD EA
