RPO3_SULAC
ID RPO3_SULAC Reviewed; 264 AA.
AC P39471; Q4JCG9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00320, ECO:0000269|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000255|HAMAP-Rule:MF_00320, ECO:0000303|PubMed:7597027};
GN Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
GN Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320,
GN ECO:0000303|PubMed:7597027}; OrderedLocusNames=Saci_0083;
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].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=7597027; DOI=10.1073/pnas.92.13.5768;
RA Langer D., Hain J., Thuriaux P., Zillig W.;
RT "Transcription in archaea: similarity to that in eucarya.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5768-5772(1995).
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_00320,
CC 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_00320,
CC ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00320};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00320};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00320}.
CC -!- CAUTION: X-ray crystallography in other archaea shows this protein
CC binds a 3Fe-4S cluster, although a 4Fe-4S cluster has been suggested to
CC be present in this protein. {ECO:0000305}.
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DR EMBL; X80194; CAA56480.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79510.1; -; Genomic_DNA.
DR PIR; S47023; S47023.
DR RefSeq; WP_011277011.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; D=1-264.
DR PDB; 7OQ4; EM; 3.27 A; D=1-264.
DR PDB; 7OQY; EM; 2.61 A; D=1-264.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P39471; -.
DR SMR; P39471; -.
DR STRING; 330779.Saci_0083; -.
DR EnsemblBacteria; AAY79510; AAY79510; Saci_0083.
DR GeneID; 3473859; -.
DR KEGG; sai:Saci_0083; -.
DR PATRIC; fig|330779.12.peg.77; -.
DR eggNOG; arCOG04241; Archaea.
DR HOGENOM; CLU_038421_3_1_2; -.
DR OMA; ECLRHPE; -.
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:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 3Fe-4S; Cytoplasm; DNA-directed RNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..264
FT /note="DNA-directed RNA polymerase subunit Rpo3"
FT /id="PRO_0000132764"
FT BINDING 203
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT BINDING 206
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT BINDING 209
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT CONFLICT 106
FT /note="P -> S (in Ref. 1; CAA56480)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7OK0"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 158..172
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7OK0"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 217..232
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 238..261
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 264 AA; 29823 MW; 385212A3C5A79DA8 CRC64;
MPISLIERNG LRLRLVLENY PLEFVNSIRR ASILYVPVMA VDEVYFIENN SPLYDEILAH
RLALVPFVSD EALEHYRPPE ECAECKENCD GCYNRVYLDV EAKDQPLMIY SRDLKSEDQM
ITPVSGAIPI VLLGSKQKIS LEARLRLGYG KEHIKYSPVS VSIVRYYPKV TVLGNCEKAV
EVCPEGVFAM ENNKLVVKNE LSCILCEECL KYCAGSVSIE SVENKFILEI ESVGSLKPER
ILIEASKSLL RKLSELKSKL EAGK
