RPO7_METJA
ID RPO7_METJA Reviewed; 187 AA.
AC Q57840;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo7 {ECO:0000255|HAMAP-Rule:MF_00865};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00865};
DE AltName: Full=DNA-directed RNA polymerase subunit E {ECO:0000255|HAMAP-Rule:MF_00865, ECO:0000303|PubMed:11741548};
DE Short=mjE {ECO:0000303|PubMed:11058130};
DE AltName: Full=DNA-directed RNA polymerase subunit E' {ECO:0000303|PubMed:8688087};
GN Name=rpo7 {ECO:0000255|HAMAP-Rule:MF_00865};
GN Synonyms=rpoE {ECO:0000255|HAMAP-Rule:MF_00865},
GN rpoE1 {ECO:0000303|PubMed:8688087}; OrderedLocusNames=MJ0397;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP INTERACTION WITH RPO4.
RX PubMed=11058130; DOI=10.1093/nar/28.21.4299;
RA Werner F., Eloranta J.J., Weinzierl R.O.;
RT "Archaeal RNA polymerase subunits F and P are bona fide homologs of
RT eukaryotic RPB4 and RPB12.";
RL Nucleic Acids Res. 28:4299-4305(2000).
RN [3] {ECO:0007744|PDB:1GO3}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), DOMAIN, AND SUBUNIT.
RX PubMed=11741548; DOI=10.1016/s1097-2765(01)00379-3;
RA Todone F., Brick P., Werner F., Weinzierl R.O., Onesti S.;
RT "Structure of an archaeal homolog of the eukaryotic RNA polymerase II
RT RPB4/RPB7 complex.";
RL Mol. Cell 8:1137-1143(2001).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00865,
CC ECO:0000269|PubMed:11741548, ECO:0000305|PubMed:11058130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00865}.
CC -!- DOMAIN: Forms 2 domains with an elongated structure; Rpo4 packs into
CC the hinge region between the 2 domains. {ECO:0000255|HAMAP-
CC Rule:MF_00865, ECO:0000269|PubMed:11741548}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00865}.
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DR EMBL; L77117; AAB98387.1; -; Genomic_DNA.
DR PIR; E64349; E64349.
DR RefSeq; WP_010869896.1; NC_000909.1.
DR PDB; 1GO3; X-ray; 1.75 A; E/M=1-187.
DR PDBsum; 1GO3; -.
DR AlphaFoldDB; Q57840; -.
DR SMR; Q57840; -.
DR IntAct; Q57840; 1.
DR STRING; 243232.MJ_0397; -.
DR EnsemblBacteria; AAB98387; AAB98387; MJ_0397.
DR GeneID; 1451254; -.
DR KEGG; mja:MJ_0397; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR InParanoid; Q57840; -.
DR OMA; MRQPGLG; -.
DR OrthoDB; 117241at2157; -.
DR PhylomeDB; Q57840; -.
DR EvolutionaryTrace; Q57840; -.
DR Proteomes; UP000000805; 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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 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; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
DR TIGRFAMs; TIGR00448; rpoE; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..187
FT /note="DNA-directed RNA polymerase subunit Rpo7"
FT /id="PRO_0000074036"
FT DOMAIN 82..166
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00865"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:1GO3"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1GO3"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:1GO3"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:1GO3"
SQ SEQUENCE 187 AA; 21216 MW; C0E4EA3C006D69DB CRC64;
MYKILEIADV VKVPPEEFGK DLKETVKKIL MEKYEGRLDK DVGFVLSIVD VKDIGEGKVV
HGDGSAYHPV VFETLVYIPE MYELIEGEVV DVVEFGSFVR LGPLDGLIHV SQIMDDYVSY
DPKREAIIGK ETGKVLEIGD YVRARIVAIS LKAERKRGSK IALTMRQPYL GKLEWIEEEK
AKKQNQE
