RPOC2_SYNP2
ID RPOC2_SYNP2 Reviewed; 1331 AA.
AC B1XHW1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
GN OrderedLocusNames=SYNPCC7002_A2043;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; CP000951; ACB00030.1; -; Genomic_DNA.
DR RefSeq; WP_012307652.1; NC_010475.1.
DR AlphaFoldDB; B1XHW1; -.
DR SMR; B1XHW1; -.
DR STRING; 32049.SYNPCC7002_A2043; -.
DR EnsemblBacteria; ACB00030; ACB00030; SYNPCC7002_A2043.
DR KEGG; syp:SYNPCC7002_A2043; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 4.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1331
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353533"
FT REGION 1236..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1331 AA; 145422 MW; C9D101BC915BB278 CRC64;
MTKEKPAVFY NRIIDKGRLK KLMSWAYTSF GSAHCATMAD ELKTLGFRYA TQAGVSISVD
DLQVPPIKRQ MLDSAEQEIK TTEARYSRGE ITEVERFQKV IDTWNSTSES LKDEVVKNFR
ETNPLNSVYM MAFSGARGNL SQVRQLVGMR GLMADPQGEI IDLPIKTNFR EGLTVTEYII
SSYGARKGLV DTALRTADSG YLTRRLVDVS QDVIVREEDC GTARGLKLRA MTDGEREQIS
LEDRLFGRVL NADVVDPKTG EVIAQRNQDI DADLAKKIAT TVAEVEVRSP LTCEAARSVC
RKCYGWSLAH GHMVDMGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTKEA ARTIKASKAG
TIQFKDGLST RRMRTPHGDE VEQVEVAGTL VLKPSDNGKM VSHALSPGSF VLVAEGASVK
KGDLLVEVGA GQKTQKSTER ATKDVSSDLA GEVLFDNLIA EEKTDRQGNT TRSAQRSGLM
WVLAGDVYNL PAGAEPVVEN GTHVNVGDIL AETKLVSLSG GVVRLIPNSR EIEIVTASVL
LDEAKVLHET GGGSEQYIIE TSKGDQFLLK TAPGTKVQNN ANIAELIDDR YRTTTGGIIK
YSGVEVAKGT KKQGYEVLKG GTLLWIPEET HEVNKDSSLR IVEDGQYVEA GTEVVKDIFS
QSAGVAEVIE KNDILREVII KPGELHLTEE AIADKYHEQL IQPGEEVIPG VTIDKLSYGE
KVISTEGVAL LVRPVEEFQV EDTPVEPSQG SINEQGAGRN IELHAVQRLF FKDGERVKSV
DGVSLLSTQL IIEIGAIEGE DEDVLANLYA DIELQDDPTD DEVKRLQLVI LESLILRRDS
DSDPFGGQVQ TRLMVEDGQE IVPGAVVART EIQCKEPGEV RGIRSGQEAI RRLLIVRDSD
RQTLAIDGKA KVKENTLVVA GTEIAEGVVI EDSAQVLKVS DKEIVLRHAR PYRVSGGAVL
HIDEGDLVQR GDNLVLLVFE RAKTGDIIQG LPRIEELLEA RKPKEAAVLA RRPGTCQVEY
LDDETVDVKV IEDDGVISEY PVSLNQSVMV VDGQRVGPAE PLTDGLNNPH EILEIFFDYY
AESKGIYEAA LIGLRESQRF LVEEVQRVYQ SQGIDISDKH IEVIVRQMTA KVRIDDGGDT
TMLPGELIEL RQVEQVNEAM SITGGAPARY TPVLLGITKA SLNTDSFISA ASFQETTRVL
TEAAIEGKSD WLRGLKENVI IGRLIPAGTG FASQNDFVDE GTSRSPNGYS NVVTNDNGAG
LSSRTYDDLD GSEILDDQTA RAFTEGKSNR KDIISGDELI SDDTPIPSDV QGKAPVIDDD
AMIDDNWMKD Q