ID D3STP7_NATMM Unreviewed; 189 AA.
AC D3STP7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo7 {ECO:0000256|HAMAP-Rule:MF_00865};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00865};
DE AltName: Full=DNA-directed RNA polymerase subunit E {ECO:0000256|HAMAP-Rule:MF_00865};
GN Name=rpoE {ECO:0000256|HAMAP-Rule:MF_00865,
GN ECO:0000313|EMBL:ADD05064.1};
GN Synonyms=rpo7 {ECO:0000256|HAMAP-Rule:MF_00865};
GN OrderedLocusNames=Nmag_1488 {ECO:0000313|EMBL:ADD05064.1};
GN ORFNames=C500_19964 {ECO:0000313|EMBL:ELY23437.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD05064.1, ECO:0000313|Proteomes:UP000001879};
RN [1] {ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000001879};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA Maupin-Furlow J.A., Woyke T.;
RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD05064.1, ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD05064.1}, and ATCC 43099 / DSM
RC 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT "A comparative genomics perspective on the genetic content of the
RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL BMC Genomics 13:165-165(2012).
RN [3] {ECO:0000313|EMBL:ELY23437.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC {ECO:0000313|EMBL:ELY23437.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:ADD05064.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD05064.1};
RA Pfeiffer F.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000256|HAMAP-Rule:MF_00865}.
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:0000256|HAMAP-Rule:MF_00865};
CC -!- SUBUNIT: Part of the RNA polymerase complex. Forms a stalk with Rpo4
CC that extends from the main structure. {ECO:0000256|HAMAP-
CC Rule:MF_00865}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00865}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- DOMAIN: Forms 2 domains with an elongated structure; Rpo4 packs into
CC the hinge region between the 2 domains. {ECO:0000256|HAMAP-
CC Rule:MF_00865}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000256|ARBA:ARBA00009307, ECO:0000256|HAMAP-
CC Rule:MF_00865}.
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DR EMBL; CP001932; ADD05064.1; -; Genomic_DNA.
DR EMBL; AOHS01000061; ELY23437.1; -; Genomic_DNA.
DR RefSeq; WP_004217296.1; NZ_AOHS01000061.1.
DR AlphaFoldDB; D3STP7; -.
DR STRING; 547559.Nmag_1488; -.
DR PaxDb; 547559-Nmag_1488; -.
DR GeneID; 8824322; -.
DR KEGG; nmg:Nmag_1488; -.
DR PATRIC; fig|547559.17.peg.3942; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR OMA; MRQPGLG; -.
DR OrthoDB; 7927at2157; -.
DR Proteomes; UP000001879; Chromosome.
DR Proteomes; UP000011543; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR CDD; cd04331; RNAP_E_N; 1.
DR CDD; cd04460; S1_RpoE; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.30.1490.120; RNA polymerase Rpb7-like, N-terminal domain; 1.
DR HAMAP; MF_00865; RNApol_arch_Rpo7; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR004519; RNAP_E/RPC8.
DR InterPro; IPR046399; RNApol_Rpo7.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00448; rpoE; 1.
DR PANTHER; PTHR12709:SF4; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7; 1.
DR PANTHER; PTHR12709; DNA-DIRECTED RNA POLYMERASE II, III; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF88798; N-terminal, heterodimerisation domain of RBP7 (RpoE); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00865};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00865};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00865,
KW ECO:0000313|EMBL:ADD05064.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001879};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:ADD05064.1}.
FT DOMAIN 82..166
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 156..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 189 AA; 20842 MW; 9312EB8664957043 CRC64;
MYKRVRLKDT VEVPPEELGD VSPTLVKRLL QDKLEGRMDE EVGSIVSVTE VRDIGEGTVL
PNRPGVYYEA DFDAVTFDPQ MQEVVDGTVV EVVEFGAFVG IGPVDGLLHV SQISDEYLAF
DAENQQLASN ESNRTLGVGD PIRARIVTKS IDERNPRDSK IGLTAKQPGL GKHDWLKSEH
EHQEATAGE
//