ID   RPO2N_HALS3             Reviewed;         523 AA.
AC   B0R8D6; P15352; Q9HM77;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo2N {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE   AltName: Full=DNA-directed RNA polymerase subunit B'' {ECO:0000303|PubMed:2495365};
GN   Name=rpo2N {ECO:0000305}; Synonyms=rpoB2 {ECO:0000303|PubMed:18313895};
GN   OrderedLocusNames=OE_4742R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, AND SUBUNIT.
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=2495365; DOI=10.1016/0022-2836(89)90519-6;
RA   Leffers H., Gropp F., Lottspeich F., Zillig W., Garrett R.A.;
RT   "Sequence, organization, transcription and evolution of RNA polymerase
RT   subunit genes from the archaebacterial extreme halophiles Halobacterium
RT   halobium and Halococcus morrhuae.";
RL   J. Mol. Biol. 206:1-17(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this
CC       organism) is implicated in DNA promoter recognition and in nucleotide
CC       binding. {ECO:0000250|UniProtKB:B8YB55}.
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:0000250|UniProtKB:P11513};
CC   -!- SUBUNIT: Part of the RNA polymerase complex.
CC       {ECO:0000269|PubMed:2495365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; X57144; CAA40424.1; -; Genomic_DNA.
DR   EMBL; AM774415; CAP15005.1; -; Genomic_DNA.
DR   PIR; S03572; S03572.
DR   RefSeq; WP_010903998.1; NC_010364.1.
DR   AlphaFoldDB; B0R8D6; -.
DR   SMR; B0R8D6; -.
DR   PRIDE; B0R8D6; -.
DR   EnsemblBacteria; CAP15005; CAP15005; OE_4742R.
DR   GeneID; 1448999; -.
DR   GeneID; 5954244; -.
DR   GeneID; 62887874; -.
DR   KEGG; hsl:OE_4742R; -.
DR   HOGENOM; CLU_000524_5_3_2; -.
DR   OMA; GKICPSE; -.
DR   PhylomeDB; B0R8D6; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
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   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; DNA-binding;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..523
FT                   /note="DNA-directed RNA polymerase subunit Rpo2N"
FT                   /id="PRO_0000409673"
FT   REGION          501..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59396 MW;  BB5CF4F80D5354E8 CRC64;
     MLQEDKRELS ESYFSKERLA EHHFRSYNAF LEHGMQDVVT EKERIETDIG DKEDEEPVWV
     ELGDVRAVTP RVREADGSEE LLYPQEARLR NITYSAPVFM EMSIVRGGEE EEERVLDTTE
     TKVGRMPIMV GSDKCNISGF SDEELIEIGE DPADPGGYFI INGSERVLMT SEDLAPNKIL
     AEYDSKYGDE IQVAKTFSQR RGYRALVLVE RNREGLLEVS FPSVSGSISF VTLVRALGLE
     SDEEIVHRVS EDPEIVKFML ENLEEADVQT QEEAIEDLGQ RVASGQGKNY QLKRANYVID
     RYLLPHLHED GVEEEETRIN KAYYLCRMAE ACFELALGRR EADDKDHYAN KRLKVSGDLM
     KDLFRTALNK LARDVKYQLE RANMRNRELT VNTVVRSDVL TERLEHPIAT GNWVGGRSGV
     SQLVDRTDFM GVLSHLRRLR SPLSRSQPHF EARDLHATQW GRICPSETPE GPNCGLVKNF
     AQAMELSQDV DDERDLKQEL SSMGVEGIPG ISMETTSTTS ADD