RPO7_SACSH
ID RPO7_SACSH Reviewed; 180 AA.
AC B8YB57;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo7 {ECO:0000255|HAMAP-Rule:MF_00865, ECO:0000303|PubMed:19419240};
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};
GN Name=rpo7 {ECO:0000255|HAMAP-Rule:MF_00865, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoE {ECO:0000255|HAMAP-Rule:MF_00865};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX, FUNCTION, SUBUNIT, DOMAIN, AND NOMENCLATURE.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA Sigler P.B., Bell S.D., Abrescia N.G.;
RT "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT structure.";
RL PLoS Biol. 7:e1000102-e1000102(2009).
RN [2] {ECO:0007744|PDB:2Y0S}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX,
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=21265742; DOI=10.1042/bst0390025;
RA Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL Biochem. Soc. Trans. 39:25-30(2011).
RN [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX,
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=22848102; DOI=10.1093/nar/gks692;
RA Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT "Structural and functional analyses of the interaction of archaeal RNA
RT polymerase with DNA.";
RL Nucleic Acids Res. 40:9941-9952(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates (Probable). The highly mobile Rpo4/Rpo7
CC heterodimer is conditionally required for transcription initiation
CC (Probable). {ECO:0000305|PubMed:19419240, ECO:0000305|PubMed:21265742,
CC ECO:0000305|PubMed:22848102}.
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:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
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:19419240,
CC ECO:0000269|PubMed:21265742, ECO:0000269|PubMed:22848102}.
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; FJ515669; ACL36492.1; -; Genomic_DNA.
DR PDB; 2WB1; X-ray; 3.52 A; E/T=1-177.
DR PDB; 2Y0S; X-ray; 3.80 A; E/T=1-180.
DR PDB; 4AYB; X-ray; 3.20 A; E=1-180.
DR PDB; 4V8S; X-ray; 4.32 A; AT/BE=1-180.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB57; -.
DR BRENDA; 2.7.7.6; 6162.
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:InterPro.
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; Transcription; Transferase.
FT CHAIN 1..180
FT /note="DNA-directed RNA polymerase subunit Rpo7"
FT /id="PRO_0000453814"
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:4AYB"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 64..77
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 180 AA; 20303 MW; DB7EA03CA4F481BD CRC64;
MYKLIKARSI VRIPPNEFGK PLNEIALNEL RQQYQEKILK DLGLVLAILN VKTSEEGMLV
FGDGATYHEV EFDMITYVPV VQEVVEGEVL QVDNYGVFVN LGPMDGLVHI SQITDDTLKY
DNVRGIIFGE KSKKVIQKGD KVRARVISVA STVTGRLPRI ALTMRQPYLG KLEWITQAKK
