RPOB_ACIBC
ID RPOB_ACIBC Reviewed; 1362 AA.
AC B2I1Z1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=ACICU_00303;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC55615.1; -; Genomic_DNA.
DR RefSeq; WP_000331899.1; NZ_CP031380.1.
DR AlphaFoldDB; B2I1Z1; -.
DR SMR; B2I1Z1; -.
DR GeneID; 66398729; -.
DR KEGG; abc:ACICU_00303; -.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000008839; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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..1362
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141649"
SQ SEQUENCE 1362 AA; 151851 MW; 59B9690BC95EB40B 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
RKVVDGRVTD 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 SLGINIELKN GD
