RPO1C_SACSH
ID RPO1C_SACSH Reviewed; 395 AA.
AC B8YB54;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000303|PubMed:19419240};
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, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX, FUNCTION, SUBUNIT, 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, AND SUBUNIT.
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 WITH
RP AND WITHOUT DNA, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
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. Forms part of the jaw domain.
CC {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000269|PubMed:19419240,
CC ECO:0000269|PubMed:21265742, ECO:0000269|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_00411};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411,
CC ECO:0000269|PubMed:22848102}.
CC -!- MISCELLANEOUS: Corresponds to about the last third of the bacterial
CC beta' subunit. {ECO:0000305|PubMed:19419240}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000305|PubMed:19419240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ515666; ACL36489.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; C=11-395.
DR PDB; 2WB1; X-ray; 3.52 A; C/Y=1-395.
DR PDB; 2Y0S; X-ray; 3.80 A; C/Y=1-395.
DR PDB; 4AYB; X-ray; 3.20 A; C=1-395.
DR PDB; 4V8S; X-ray; 4.32 A; AY/BC=1-395.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB54; -.
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: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; Transcription; Transferase.
FT CHAIN 1..395
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_0000453786"
FT BINDING 109..118
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 115
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 148
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 192
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 221..229
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 328..332
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 331..332
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 348..353
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 395 AA; 43732 MW; 2E3CAE06113DD36E CRC64;
MENVIDEKDK SYLEEKVKQA SNILPQKIVE DLKNLISNKE VLVTRDEIDK IFDLAIKEYS
EGLIAPGEAI GIVAAQSVGE PGTQMTLRTF HFAGIRELNV TLGLPRLIEI VDAKKVPSTP
MMTIYLTDEY KHDKEKALEV ARKLEYTKIE NVVSSTSIDI ASMSIILQLD NEMLKDKGVT
VDDVKKAINR LKLGEFVIDE SEGNTLNISF ANIDSIAALF KLRDKILNTK IKGIKGIKRA
IVQKKGDEYI ILTDGSNLSG VLSVKGVDIA KVETNNIREI EEVFGIEAAR EIIIREISKV
LAEQGLDVDM RHILLVADVM TRTGVVRQIG RHGVTGEKNS VLARAAFEVT VKHLLDAAAR
GDVEEFKGVV ENIIIGHPIK LGTGMVELTM RPILR
