RPO7_SACS2
ID RPO7_SACS2 Reviewed; 180 AA.
AC Q980A3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
DE AltName: Full=DNA-directed RNA polymerase, subunit E' {ECO:0000303|PubMed:18235446};
GN Name=rpo7 {ECO:0000255|HAMAP-Rule:MF_00865};
GN Synonyms=rpoE {ECO:0000255|HAMAP-Rule:MF_00865}; OrderedLocusNames=SSO0415;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND
RP SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18235446; DOI=10.1038/nature06530;
RA Hirata A., Klein B.J., Murakami K.S.;
RT "The X-ray crystal structure of RNA polymerase from Archaea.";
RL Nature 451:851-854(2008).
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 13-subunit RNA polymerase complex. Forms a stalk
CC with Rpo4 that extends from the main structure.
CC {ECO:0000269|PubMed:18235446}.
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:18235446}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00865}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006641; AAK40742.1; -; Genomic_DNA.
DR PIR; G90185; G90185.
DR RefSeq; WP_009988767.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; E/T=1-180.
DR PDB; 3HKZ; X-ray; 3.40 A; E/Q=1-180.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR SMR; Q980A3; -.
DR DIP; DIP-60644N; -.
DR IntAct; Q980A3; 1.
DR STRING; 273057.SSO0415; -.
DR EnsemblBacteria; AAK40742; AAK40742; SSO0415.
DR GeneID; 44129394; -.
DR KEGG; sso:SSO0415; -.
DR PATRIC; fig|273057.12.peg.409; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR InParanoid; Q980A3; -.
DR OMA; MRQPGLG; -.
DR PhylomeDB; Q980A3; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; Q980A3; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
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..180
FT /note="DNA-directed RNA polymerase subunit Rpo7"
FT /id="PRO_0000453813"
FT DOMAIN 82..165
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00865"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2PMZ"
SQ SEQUENCE 180 AA; 20329 MW; 2351BE9ADA4847C7 CRC64;
MYKLIKARSI VRIPPNEFGK PLNEIALNEL RQQYQEKILK DLGLVLAILN VKTSEEGILV
FGDGATYHEV EFDMITYVPV VQEVVEGEVL QVDNYGIFVN LGPMDGLVHI SQITDDTLKY
DNVRGIIFGE KSKKVIQKGD KVRARVISVA STVTGRLPRI ALTMRQPYLG KLEWITQTKK
