RPOB_ACIBT
ID RPOB_ACIBT Reviewed; 1357 AA.
AC A3M1G3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=A1S_0287;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO10757.2; -; Genomic_DNA.
DR AlphaFoldDB; A3M1G3; -.
DR SMR; A3M1G3; -.
DR PRIDE; A3M1G3; -.
DR KEGG; acb:A1S_0287; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR PHI-base; PHI:7860; -.
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..1357
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300271"
SQ SEQUENCE 1357 AA; 151324 MW; FF05A25391D02FE5 CRC64;
MAYSYTEKKR IRKNFGKLPQ VMDAPYLLSI QVDSYRTFLQ DGKSPKNRED IGLQAAFRSV
FPIESYSGNA ALEFVEYSLG KPEFDVRECI LRGSTYAAPM RVKIRLIIKD RETKSIKDVR
EQEVYMGEIP LMTENGTFVI NGTERVIVSQ LHRSPGVFFD HDKGKTHSSG KVLYSARIIP
YRGSWLDFEF DAKDLVYVRI DRRRKLLATV VLRALGYNNE QILNLFYEKV PVYLDMGSYQ
IDLVPERLRG EMAQFDITDN EGKVIVEQGK RINARHVRQM EAAGLTKLSV PDEYLYERIT
AEDITLRDGE VIAANTLLSH EVMVKLAEGG VKQFNILFTN DIDRGSFVAD TLRADLTRDR
EEALVEIYKV MRPGEPPTKE AAENLFNNLF FSSERYDLSP VGRMKFNRRL GRPYEVGTDQ
KSREVEGILS HEDIIDVLRT LVEIRNGKGE VDDIDHLGNR RVRSVGEMTE NQFRVGLVRV
ERAVKERLSQ AETDNLSPQD LINAKPVAAA IKEFFGSSQL SQFMDQNNPL SEITHKRRVS
ALGPGGLTRE RAGFEVRDVH QTHYGRVCPI ETPEGPNIGL INSLSVYAKA NDFGFLETPY
RKVIDGRVTD DVEYLSAIEE VGTVIAQADS AVDKDGNLTE EFVSVRHQGE FVRMPPEKVT
HMDVSAQQVV SVAASLIPFL EHDDANRALM GSNMQRQAVP TLRADKPLVG TGMEANVARD
SGVCVIANRG GVIEYVDASR IVIRVNEDEM VAGEAGVDIY NLIKYTRSNQ NTCINQNVIV
NLGDKVARGD ILADGPSTDM GELALGQNMR VAFMTWNGYN YEDSILLSER VLQEDRLTSI
HIQELSCVAR DTKLGAEEIT ADIPNVGEAA LSKLDESGIV YIGAEVTAGD ILVGKVTPKG
ETQLTPEEKL LRAIFGEKAA DVKDSSLRVP SGTKGTVIDV QVFTRDGLEK DDRALAIEKA
QLDSYRKDLK EEYKIFEEAA RERVIRLLKG QESNGGGSTK RGDKLSEDLL SGLELVDLLE
IQPADEAIAE RLTQIQVFLK EKSAEIDEKF AEKKRKLATG DELTTGVLKV VKVYLAVKRR
IQPGDKMAGR HGNKGVVSNI LPVEDMPHDA NGVPVDIVLN PLGVPSRMNV GQILETHLGM
AAKGLGDKIE KMLKEQRTVL ELREFLDKIY NKVGGEQEDL DSLTDEEILA LAGNLRAGVP
LATPVFDGAE ESQIKDLLEL ADISRTGQTV LFDGRTGEQF DRPVTVGYMY MLKLNHLVDD
KMHARSTGSY SLVTQQPLGG KAQFGGQRFG EMEVWALEAY GAAYTLQEML TVKSDDVEGR
TRIYKNIVDG NHYMDPGMPE SFNVLTKEIR SLGINID
