RPO7_SULAC
ID RPO7_SULAC Reviewed; 183 AA.
AC P39466; Q4JAH8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
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, ECO:0000269|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit E {ECO:0000255|HAMAP-Rule:MF_00865};
GN Name=rpo7 {ECO:0000255|HAMAP-Rule:MF_00865};
GN Synonyms=rpoE {ECO:0000255|HAMAP-Rule:MF_00865};
GN OrderedLocusNames=Saci_0834;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8127719; DOI=10.1093/nar/22.4.694;
RA Langer D., Lottspeich F., Zillig W.;
RT "A subunit of an archaeal DNA-dependent RNA polymerase contains the S1
RT motif.";
RL Nucleic Acids Res. 22:694-694(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1729711; DOI=10.1073/pnas.89.1.407;
RA Klenk H.-P., Palm P., Lottspeich F., Zillig W.;
RT "Component H of the DNA-dependent RNA polymerases of Archaea is homologous
RT to a subunit shared by the three eucaryal nuclear RNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:407-410(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX DOI=10.1016/S0723-2020(11)80337-1;
RA Lanzendorfer M., Langer D., Hain J., Klenk H.-P., Holz I., Arnold-Ammer I.,
RA Zillig W.;
RT "Structure and Function of the DNA-Dependent RNA Polymerase of
RT Sulfolobus.";
RL Syst. Appl. Microbiol. 16:656-664(1994).
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 ECO:0000269|Ref.4}.
CC -!- FUNCTION: Reconstitution experiments show this subunit is required for
CC basic activity. {ECO:0000269|Ref.4}.
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 ECO:0000269|Ref.4};
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:1729711, ECO:0000269|Ref.4}.
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}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00865}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53164.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X75411; CAA53164.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000077; AAY80201.1; -; Genomic_DNA.
DR PIR; S42389; S38658.
DR RefSeq; WP_011277703.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; E=1-183.
DR PDB; 7OQ4; EM; 3.27 A; E=1-183.
DR PDB; 7OQY; EM; 2.61 A; E=1-183.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P39466; -.
DR SMR; P39466; -.
DR STRING; 330779.Saci_0834; -.
DR EnsemblBacteria; AAY80201; AAY80201; Saci_0834.
DR GeneID; 3472705; -.
DR KEGG; sai:Saci_0834; -.
DR PATRIC; fig|330779.12.peg.798; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR OMA; MRQPGLG; -.
DR BRENDA; 2.7.7.6; 6160.
DR Proteomes; UP000001018; 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; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..183
FT /note="DNA-directed RNA polymerase subunit Rpo7"
FT /id="PRO_0000074038"
FT DOMAIN 82..164
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00865"
FT CONFLICT 137
FT /note="Q -> T (in Ref. 1; CAA53164)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> R (in Ref. 1; CAA53164)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7OQ4"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 183 AA; 20471 MW; DA621E0357A2E2B9 CRC64;
MFKLVRAKGI VRIPPEYFGQ SVDEIAIKIL RQEYQEKLIK DIGVVLGIVN AKASEEGFII
FGDGATYHEV EFDMLVYTPI IHEVIEGEVS QVDNYGVYVN MGPVDGLVHI SQITDDNLKF
DSNRGILIGE KSKKSIQKGD RVRAMIISAS MSSGRLPRIA LTMKQPYLGK IEWINQEIAK
ASK
