RPO2C_HALS3
ID RPO2C_HALS3 Reviewed; 608 AA.
AC B0R8D5; P15351; Q9HM78;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2C {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=rpo2C {ECO:0000305}; Synonyms=rpoB1 {ECO:0000303|PubMed:18313895};
GN OrderedLocusNames=OE_4741R;
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 2-13, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:B8YB55};
CC Note=Binds 1 Zn(2+) per subunit. {ECO:0000250|UniProtKB:B8YB55};
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; CAA40425.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP15004.1; -; Genomic_DNA.
DR PIR; S03573; S03573.
DR RefSeq; WP_010903997.1; NC_010364.1.
DR AlphaFoldDB; B0R8D5; -.
DR SMR; B0R8D5; -.
DR PRIDE; B0R8D5; -.
DR EnsemblBacteria; CAP15004; CAP15004; OE_4741R.
DR GeneID; 5954242; -.
DR KEGG; hsl:OE_4741R; -.
DR HOGENOM; CLU_000524_2_2_2; -.
DR OMA; YQKLYHM; -.
DR PhylomeDB; B0R8D5; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 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; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR019969; RNAP_Rpo2.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA-binding;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Transcription; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2495365"
FT CHAIN 2..608
FT /note="DNA-directed RNA polymerase subunit Rpo2C"
FT /id="PRO_0000409672"
FT REGION 278..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 67276 MW; DDD24AC5DC7B1435 CRC64;
MSTEREAKVY VNGSLVGTHE NPEELAEQIR EARRRGEVSE MVNVSVRDRT GEVIVNADAG
RARRPLLVVE NGEPVVTQEE VEAVKNGDID FEDLVEAGKV EFIDAEEEED ILVGVEEEEL
TTDHTHLEID PQLIFGIGAG MIPYPEHNAS PRITMGAGMM KQSLGLPAAN YRIRPDTRQH
LLHYPQKAMV NTQTTEQIGY DDRPAGQNFV VAVMSYEGFN IEDALVMNKG SVERALSRSH
FFRTYEGEER RYPGGQEDRF EIPGDDVRGA RGEDAYTHLD DDGLVNPETK VDDSSVLLGK
TSPPRFLEEP EDMGGLSPQK RRETSVTMRS GEDGVVDTVT LMEGEDGSKL AKVSVRDERI
PELGDKFASR HGQKGVVGHL APQEDMPFTQ EGVVPDLVLN PHALPSRMTV GHVLEMLGGK
AGSLDGRSVD GTPFTGEGED EIRGTLEDRG FKSSGKEVMY SGVSGEKIEA EIFVGTIFYH
KLYHMVSNKL HARSKGPVQV LTRQPTEGRA REGGLRVGEM ERDTVIGHGA AMVLKERLLD
SSDREEIHVC GNCGMTAVEN YEQRRVYCPN CEEETDVHSI EMSYAFKLLL DEMKALGIAP
RLELEEAV
