ID RPO2_SACS2 Reviewed; 1124 AA. AC Q980R1; Q980R0; DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot. DT 29-SEP-2021, sequence version 2. DT 24-JAN-2024, entry version 133. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2 {ECO:0000305}; DE EC=2.7.7.6 {ECO:0000305|PubMed:18235446}; DE AltName: Full=DNA-directed RNA polymerase subunit B {ECO:0000303|PubMed:18235446}; GN Name=rpo2 {ECO:0000305}; GN Synonyms=rpoB1 {ECO:0000303|PubMed:11427726}, rpoB2 GN {ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0227/SSO3254; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; 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 (3.40 ANGSTROMS) OF 479-1124 OF THE RNA POLYMERASE RP COMPLEX IN COMPLEX WITH ZINC, SEQUENCE REVISION, FUNCTION, COFACTOR, AND RP SUBUNIT. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; 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 (Probable). This subunit is involved in DNA CC promoter recognition (By similarity). {ECO:0000250|UniProtKB:B8YB55, CC ECO:0000305|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:0000305|PubMed:18235446}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:18235446}; CC Note=Binds 1 Zn(2+) per subunit. {ECO:0000269|PubMed:18235446}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. CC {ECO:0000269|PubMed:18235446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK40567.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAK40568.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AE006641; AAK40568.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE006641; AAK40567.1; ALT_FRAME; Genomic_DNA. DR PIR; A99164; A99164. DR PIR; H90163; H90163. DR PDB; 2PMZ; X-ray; 3.40 A; B/R=5-1124. DR PDB; 3HKZ; X-ray; 3.40 A; B/J=5-1119. DR PDBsum; 2PMZ; -. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; Q980R1; -. DR SMR; Q980R1; -. DR DIP; DIP-60640N; -. DR IntAct; Q980R1; 1. DR STRING; 273057.SSO3254; -. DR PaxDb; 273057-SSO0227; -. DR EnsemblBacteria; AAK40567; AAK40567; SSO0227. DR EnsemblBacteria; AAK40568; AAK40568; SSO3254. DR KEGG; sso:SSO0227; -. DR KEGG; sso:SSO3254; -. DR PATRIC; fig|273057.12.peg.223; -. DR eggNOG; arCOG01762; Archaea. DR HOGENOM; CLU_000524_2_2_2; -. DR InParanoid; Q980R1; -. DR PhylomeDB; Q980R1; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; Q980R1; -. 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-KW. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1070.20; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom. DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR InterPro; IPR019969; RNAP_Rpo2. DR NCBIfam; TIGR03670; rpoB_arch; 1. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF7; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase; KW Metal-binding; Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase; Zinc. FT CHAIN 1..1124 FT /note="DNA-directed RNA polymerase subunit Rpo2" FT /id="PRO_0000453793" FT BINDING 1061 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18235446, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT BINDING 1064 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18235446, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT BINDING 1079 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18235446, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT BINDING 1082 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:B8YB55" FT HELIX 8..18 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 28..36 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 86..89 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 135..141 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 169..175 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 207..210 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 223..229 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 235..242 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 287..294 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 305..308 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 312..322 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 323..327 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 346..372 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 374..377 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 387..391 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 392..395 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 396..398 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 418..427 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 450..452 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 462..466 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 483..485 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 486..490 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 491..493 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 520..524 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 526..529 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 536..543 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 544..547 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 554..557 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 566..569 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 572..575 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 577..581 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 583..585 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 591..595 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 604..609 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 612..616 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 621..623 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 630..633 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 644..647 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 651..653 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 663..672 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 673..675 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 682..686 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 690..693 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 702..704 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 707..711 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 713..715 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 718..722 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 734..736 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 740..742 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 743..746 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 747..750 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 754..760 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 765..768 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 778..782 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 789..791 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 803..805 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 809..811 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 845..854 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 860..867 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 877..879 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 887..892 FT /evidence="ECO:0007829|PDB:3HKZ" FT TURN 894..896 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 897..899 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 907..910 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 912..914 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 916..918 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 923..931 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 934..938 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 950..959 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 970..972 FT /evidence="ECO:0007829|PDB:3HKZ" FT TURN 973..975 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 988..994 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 997..999 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 1011..1013 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 1020..1022 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 1027..1029 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 1030..1032 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 1034..1037 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 1038..1040 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 1042..1053 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 1057..1061 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 1062..1064 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 1073..1075 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 1083..1086 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 1088..1092 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 1095..1106 FT /evidence="ECO:0007829|PDB:2PMZ" SQ SEQUENCE 1124 AA; 126552 MW; 03FED53462D84CFF CRC64; MASNLTIDER WRVIEAYFKS KGLVRQHLDS YNDFVRNKLQ EIIDEQGEIP TEIPGLKVRL GKIRIGKPRV RESDRGEREI SPMEARLRNL TYAAPLWLTM IPVENNIEAE PEEVYIGDLP IMLKSAIDPI SQYTLDKLIE IGEDPKDPGG YFIVNGSERV IVTQEDLAPN RVLVDTGKTG SNITHTAKII SSTAGYRVPV TIERLKDGTF HVSFPAVPGK IPFVILMRAL GILTDRDIVY AVSLDPEVQN ELFPSLEQAS SIANVDDALD FIGSRVAIGQ KRENRIEKAQ QIIDKYFLPH LGTSAEDRKK KAYYLAYAIS KVIELYLGRR EPDDKDHYAN KRLRLAGDLF ASLFRVAFKA FVKDLTYQLE KSKVRGRKLA LKALVRPDIV TERIRHALAT GNWVGGRTGV SQLLDRTNWL SMLSHLRRVI SSLARGQPNF EARDLHGTQW GRMCPFETPE GPNSGLVKNL ALMAQIAVGI NERIVEKTLY EMGVVPVEEV IRRVTEGGED QNEYLKWSKV ILNGRLIGYY QDGGELANKI RERRRKGEIS DEVNVGHIVT DFINEVHVNC DSGRVRRPLI IVSNGNPLVT IEDIEKLESG AITFDDLVRQ GKIEYLDAEE EENAYVALEP NDLTPDHTHL EIWSPAILGI TASIIPYPEH NQSPRNTYQS AMAKQALGLY AANYQLRTDT RAHLLHYPQR PLVQTRALDI IGYTNRPAGN NAILAVMSFT GYNMEDSIIM NRSSVERGMY RSTFFRLYST EEVKYPGGQE DKIVMPEAGV RGYKGKEYYR LLEDNGVVSP EVEVKGGDVL IGKVSPPRFL QEFKELSPEQ AKRDTSIVTR HGEMGIVDLV LITETAEGNK LVKVRVRDLR IPTIGDKFAS RHGQKGVIGM LIPQVDMPYT VKGVVPDIIL NPHALPSRMT LGQIMEGIAG KYAALSGNIV DATPFYKTPI EQLQNEILRY GYLPDATEVV YDGRTGQKIK SRIYFGVVYY QKLHHMVADK LHARARGPVQ ILTRQPTEGR AREGGLRFGE MERDCLIGFG TAMLLKDRLL DNSDRTMIYV CDQCGYIGWY DKNKNKYVCP IHGDKSNLFP VTVSYAFKLL IQELMSMIIS PRLVLEDKVG LSGG //