RPO1C_HALS3
ID RPO1C_HALS3 Reviewed; 397 AA.
AC B0R8D3; P15354; Q9HM80;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
DE AltName: Full=DNA-directed RNA polymerase subunit C {ECO:0000303|PubMed:2495365};
DE Short=Subunit C {ECO:0000303|PubMed:2495365};
GN Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411};
GN OrderedLocusNames=OE_4739R;
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 2-10, 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. Forms part of the jaw domain.
CC {ECO:0000255|HAMAP-Rule:MF_00411}.
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_00411};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00411, ECO:0000269|PubMed:2495365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR EMBL; X57144; CAA40427.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP15002.1; -; Genomic_DNA.
DR PIR; S03577; S03577.
DR RefSeq; WP_010903995.1; NC_010364.1.
DR AlphaFoldDB; B0R8D3; -.
DR SMR; B0R8D3; -.
DR PRIDE; B0R8D3; -.
DR EnsemblBacteria; CAP15002; CAP15002; OE_4739R.
DR GeneID; 5954046; -.
DR KEGG; hsl:OE_4739R; -.
DR HOGENOM; CLU_037097_1_0_2; -.
DR OMA; TPMMTVY; -.
DR PhylomeDB; B0R8D3; -.
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-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd06528; RNAP_A; 1.
DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR012757; RPO1C.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA-binding;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2495365"
FT CHAIN 2..397
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_1000194737"
SQ SEQUENCE 397 AA; 43750 MW; 453E5DBAEC78A1DC CRC64;
MTEFDVTDGV HDVIEDTELP RRLKDEVLAT AEERGVTKSQ ANEIATAVEA QYLDTRVDPL
DPVGTVSAQS IGEPGTQMTM NTFHYAGVAE MDVTQGLPRL IELVDARKTP DTPVMEVYLE
DEYAEERERA HEVVWKIEAT KILALGDIST NVADMVVRID LNEDTLQERW PRVDSTTQIA
GEVAETIEGN LGVTVTQDGT ILEFGPSEPS YRELLQLVEQ LRDIVFKGIE EVSRVVIRRE
ETERGEEFVL YTEGSAFKKA LKIEGVDATR TSCNNIHEVH KTLGIEAARE AIINETMTTL
EEQGLDDVNI RHLMLVADIM TNDGTIESIG RHGISGNKNS VLARAAFEVT VNHLLDAAIH
GESDDLDGVI ENVIVGKPVR LGTGDVDLRM GATQTSD