ID S5QF32_OSTTA Unreviewed; 1011 AA.
AC S5QF32;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:AGR88202.1};
GN ORFNames=OtCpg00280 {ECO:0000313|EMBL:AGR88202.1};
OS Ostreococcus tauri.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGR88202.1}.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:AGR88202.1};
RN [1] {ECO:0000313|EMBL:AGR88202.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCC1110 {ECO:0000313|EMBL:AGW30565.1}, RCC1112
RC {ECO:0000313|EMBL:AGW30626.1}, RCC1117 {ECO:0000313|EMBL:AGW30872.1},
RC RCC1118 {ECO:0000313|EMBL:AGW30933.1}, RCC1123
RC {ECO:0000313|EMBL:AGW30994.1}, RCC1558 {ECO:0000313|EMBL:AGW31055.1},
RC RCC1559 {ECO:0000313|EMBL:AGW31116.1}, and RCC1561
RC {ECO:0000313|EMBL:AGW31177.1};
RX PubMed=23873918; DOI=10.1093/gbe/evt106;
RA Blanc-Mathieu R., Sanchez-Ferandin S., Eyre-Walker A., Piganeau G.;
RT "Organellar Inheritance in the Green Lineage: Insights from Ostreococcus
RT tauri.";
RL Genome Biol. Evol. 5:1503-1511(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; KC990831; AGR88202.1; -; Genomic_DNA.
DR EMBL; KF285523; AGW30565.1; -; Genomic_DNA.
DR EMBL; KF285524; AGW30626.1; -; Genomic_DNA.
DR EMBL; KF285528; AGW30872.1; -; Genomic_DNA.
DR EMBL; KF285529; AGW30933.1; -; Genomic_DNA.
DR EMBL; KF285530; AGW30994.1; -; Genomic_DNA.
DR EMBL; KF285531; AGW31055.1; -; Genomic_DNA.
DR EMBL; KF285532; AGW31116.1; -; Genomic_DNA.
DR EMBL; KF285533; AGW31177.1; -; Genomic_DNA.
DR RefSeq; YP_717231.1; NC_008289.1.
DR AlphaFoldDB; S5QF32; -.
DR SMR; S5QF32; -.
DR GeneID; 4238800; -.
DR KEGG; ota:OstapCp28; -.
DR OrthoDB; 1104155at2759; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; IPR007066; RNA_pol_Rpb1_3.
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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AGR88202.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AGR88202.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Zinc {ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 4..58
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 87..165
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 168..446
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 875..924
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1011 AA; 113458 MW; 2858C2002DFDB9EA CRC64;
MKTFFCNRTV DKGEMKRLIK WVLLNYGTEK TTRLIDKLKT MGFHYATHAG ISLGIDDLSI
PPIKSAFLLN AENDIYENDL RLKRGQITSV QRLEKALDIW NTTNDTLKTE VVKYFRSTDI
FNPVYMMAFS GARGNISQVR QLVGMRGLMA DPQGQILDFP IRRNFREGLT VTEYMISCYG
ARKGLVDTAL RTASSGYLTR RLVDVAQSVI IQQVDCQTTQ GLRIVPELEK IESQLIGRVL
FEDVVDLETG RMVGYKNQDI SPALALKLIK QPALTIRSPL TCRFHAVCQL CYGWNLAQQK
LVQLGEAVGV LAAQSIGEPG TQLTMRTFHT GGVFAGEATE KVYSPHNGIV FYSKQARGRK
IVSKYGEVAF LTFEPLKVKI KNDNTTSVLE FPSFTLLYIP PGQTVGEHQS LAELSRIENK
QNFQQFEVGT ENVQKEFMSN CSGQIFLPQR QNALINEDNA GTTTFNYSEM WLLAGKILDS
KTLVPGDQIK NALYPIRSKI NCEPSRLTTT LPLGYVFPID SNQTSLSKLQ STDAETLKQL
PLLQFSKLSA DNLKFARSYA LELNKTLFHC DSLSKYRFIT SDLEHLPFKS KNLFFNQDTP
TKKVPTFKIK FSRFGKADKF NAKEKFLLLR SVTKLVSTQT NPLKTQFANN LFVQNSINKN
KKTFLEVVKP LKTFQKKTNF FPSPTHENIK SFNPSLQNGN LMSVDADYVR LNVQYGKGFS
SLLNCGEVRA TNCMMTEKDQ IAFKSPVCDL KMKVGDYARV EDQLTTSTRI PLSGQINFIT
AENVLFRSVQ PYLLVPGSNV VVKHGSLVQE NSVLGTLMTS QSTAGDIVQG LPKVDELLEA
REPQHKVLTS MHAKLSTLFS QYGKIYGLRE GCELSFQKIR QFLVQEVQDV YQSQGVYIGD
KHVEIIVRQM TTHVVVVDAG KTGLLPGDIV DIRRIEQLEH TGFFAGVKYR PMLLGITRAA
LMAESFISAA SFQETKRVLS KAALEGQIDW LTGLKENVIL GRLIPAGTGL Y
//
