RPO1C_SULAC
ID RPO1C_SULAC Reviewed; 393 AA.
AC P11514; Q4JAV8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000303|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000303|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit C {ECO:0000303|PubMed:2501756};
DE Short=Subunit C;
GN Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411,
GN ECO:0000303|PubMed:1729711}, rpoC {ECO:0000303|PubMed:2501756};
GN OrderedLocusNames=Saci_0691;
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=2501756; DOI=10.1093/nar/17.12.4517;
RA Puehler G., Lottspeich F., Zillig W.;
RT "Organization and nucleotide sequence of the genes encoding the large
RT subunits A, B and C of the DNA-dependent RNA polymerase of the
RT archaebacterium Sulfolobus acidocaldarius.";
RL Nucleic Acids Res. 17:4517-4534(1989).
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. Forms part of the jaw domain.
CC {ECO:0000255|HAMAP-Rule:MF_00411, 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_00411,
CC ECO:0000269|Ref.4};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000305}.
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DR EMBL; X14818; CAA32926.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80071.1; -; Genomic_DNA.
DR PIR; S04718; S04718.
DR RefSeq; WP_011277573.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; C=1-393.
DR PDB; 7OQ4; EM; 3.27 A; C=1-393.
DR PDB; 7OQY; EM; 2.61 A; C=1-393.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P11514; -.
DR SMR; P11514; -.
DR STRING; 330779.Saci_0691; -.
DR EnsemblBacteria; AAY80071; AAY80071; Saci_0691.
DR GeneID; 3472537; -.
DR KEGG; sai:Saci_0691; -.
DR PATRIC; fig|330779.12.peg.659; -.
DR eggNOG; arCOG04256; Archaea.
DR HOGENOM; CLU_037097_1_0_2; -.
DR OMA; TPMMTVY; -.
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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd06528; RNAP_A; 1.
DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR012757; RPO1C.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..393
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_0000074025"
FT CONFLICT 226..235
FT /note="NTKIKGVKGI -> IQDKGSQGY (in Ref. 1; CAA32926)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="I -> M (in Ref. 1; CAA32926)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7OK0"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 238..253
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:7OK0"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 393 AA; 44444 MW; F7AA444ABAF088CC CRC64;
MIDEKLKGYI DKRLNEIKDK IPDKLHEDLR AAIMDINGVE LTEEDIDRII DLTIREYQQS
LIEPGEAIGV VTAQSVGEPG TQMTLRTFHF AGIRELNVTL GLPRLIEIVD ARKVPSTPMM
TIYLTDEYKT DKDKALDIAR RIEYTRVENV VSSVSVDISN MSITLQFDQE MLKDKGVSIE
EIKKIITKLK LGEIRIEDND EYSFTIYFEK IDSIMALFKM REKILNTKIK GVKGIKRAIV
QKKGDEYVII TDGSNLEGIM NVTGVDINKI QTNNIHEVEE VLGIEAAREL ISREIKKVLE
EQGLDVDMRH IVLVSDIMTR TGDIRQIGRH GVTGEKSSVL ARAAFEVTVK HLLDAAARGE
REEFKGVIEN IIIGQPIRLG TGIVELTMKP NMR
