RPO1C_SACS2
ID RPO1C_SACS2 Reviewed; 392 AA.
AC P58192;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
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};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
GN Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411};
GN OrderedLocusNames=SSO0223;
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 (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX,
RP FUNCTION, AND SUBUNIT.
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. Forms part of the jaw domain.
CC {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000269|PubMed:18235446}.
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 -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:18235446}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40565.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40565.1; ALT_INIT; Genomic_DNA.
DR PIR; F90163; F90163.
DR RefSeq; WP_009990475.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; C/G=1-392.
DR PDB; 3HKZ; X-ray; 3.40 A; C/M=1-392.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR AlphaFoldDB; P58192; -.
DR SMR; P58192; -.
DR DIP; DIP-60639N; -.
DR IntAct; P58192; 1.
DR STRING; 273057.SSO0223; -.
DR EnsemblBacteria; AAK40565; AAK40565; SSO0223.
DR GeneID; 44129194; -.
DR KEGG; sso:SSO0223; -.
DR PATRIC; fig|273057.12.peg.220; -.
DR eggNOG; arCOG04256; Archaea.
DR HOGENOM; CLU_037097_1_0_2; -.
DR InParanoid; P58192; -.
DR OMA; TPMMTVY; -.
DR PhylomeDB; P58192; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; P58192; -.
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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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..392
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_0000074026"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:3HKZ"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2PMZ"
SQ SEQUENCE 392 AA; 43488 MW; 5B0E871D056CE08B CRC64;
MIDEKDKPYL EEKVKQASNI LPQKIVDDLK NLILNKEIIV TRDEIDKIFD LAIKEYSEGL
IAPGEAIGIV AAQSVGEPGT QMTLRTFHFA GIRELNVTLG LPRLIEIVDA KKVPSTPMMT
IYLTDEYKRD RDKALEVARK LEYTKIENVV SSTSIDIASM SIILQLDNEM LKDKGVTVDD
VKKAIGRLKL GDFMIEESED STLNINFANI DSIAALFKLR DKILNTKIKG IKGIKRAIVQ
KKGDEYIILT DGSNLSGVLS VKGVDVAKVE TNNIREIEEV FGIEAAREII IREISKVLAE
QGLDVDIRHI LLIADVMTRT GIVRQIGRHG VTGEKNSVLA RAAFEVTVKH LLDAAARGDV
EEFKGVVENI IIGHPIKLGT GMVELTMRPI LR
