RPO12_SACSH
ID RPO12_SACSH Reviewed; 48 AA.
AC B8YB64;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo12 {ECO:0000255|HAMAP-Rule:MF_00615, ECO:0000303|PubMed:19419240};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00615};
DE AltName: Full=DNA-directed RNA polymerase subunit P {ECO:0000255|HAMAP-Rule:MF_00615};
GN Name=rpo12 {ECO:0000255|HAMAP-Rule:MF_00615, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoP {ECO:0000255|HAMAP-Rule:MF_00615};
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 (3.52 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT, AND
RP 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 IN
RP COMPLEX WITH ZINC, COFACTOR, 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 IN
RP COMPLEX WITH ZINC WITH AND WITHOUT DNA, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
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. {ECO:0000255|HAMAP-Rule:MF_00615}.
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_00615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00615,
CC ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
CC ECO:0007744|PDB:4V8S};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00615,
CC ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
CC ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
CC ECO:0007744|PDB:4V8S};
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_00615,
CC ECO:0000269|PubMed:22848102}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA
CC polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00615}.
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DR EMBL; FJ515676; ACL36499.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; P=6-48.
DR PDB; 2WB1; X-ray; 3.52 A; P/X=1-48.
DR PDB; 2Y0S; X-ray; 3.80 A; P/X=1-48.
DR PDB; 4AYB; X-ray; 3.20 A; P=1-48.
DR PDB; 4V8S; X-ray; 4.32 A; AX/BP=1-48.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB64; -.
DR GeneID; 8761752; -.
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:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00615; RNApol_arch_Rpo12; 1.
DR InterPro; IPR006591; RNAP_P/RPABC4.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR023464; Rpo12.
DR SMART; SM00659; RPOLCX; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..48
FT /note="DNA-directed RNA polymerase subunit Rpo12"
FT /id="PRO_0000453879"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19419240,
FT ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615,
FT ECO:0000269|PubMed:19419240, ECO:0007744|PDB:2WAQ,
FT ECO:0007744|PDB:2WB1, ECO:0007744|PDB:2Y0S,
FT ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 48 AA; 5597 MW; C822E342B8BEFF21 CRC64;
MAVYRCGKCW KTFTDEQLKV LPGVRCPYCG YKIIFMVRKP TIKIVKAI
