RPO2_SACS2
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 03-AUG-2022, entry version 125.
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},
GN rpoB2 {ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0227/SSO3254;
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 (3.40 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};
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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 SMR; Q980R1; -.
DR DIP; DIP-60640N; -.
DR IntAct; Q980R1; 1.
DR STRING; 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 OMA; YQKLYHM; -.
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:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 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 PANTHER; PTHR20856; PTHR20856; 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 TIGRFAMs; TIGR03670; rpoB_arch; 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
