RPOC_BDEBA
ID RPOC_BDEBA Reviewed; 1375 AA.
AC Q6MJ10;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Bd2983;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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_01322}.
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_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; BX842654; CAE80753.1; -; Genomic_DNA.
DR RefSeq; WP_011165357.1; NC_005363.1.
DR AlphaFoldDB; Q6MJ10; -.
DR SMR; Q6MJ10; -.
DR STRING; 264462.Bd2983; -.
DR PRIDE; Q6MJ10; -.
DR EnsemblBacteria; CAE80753; CAE80753; Bd2983.
DR KEGG; bba:Bd2983; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008080; 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:0000287; F:magnesium ion binding; 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 Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1375
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067709"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 881
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1375 AA; 151750 MW; 03C381F6D4A6ED0B CRC64;
MRDLLNFFDK PKDPLSFDAV RVSLASPEMI REWSFGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRMKY RGVVCEKCGV EVTQTKVRRE RLGHIELATP VAHIWFLRSL
PSRIGNLLNL SLKDVEKVLY CEAHVVIDPM ETTLEEGQVL TEEALQAALN EFGPSFKYGM
GGEAVRDLLK KIDPEYLSRK LRLEVKDTKS EAGIKKLTKR LRVVEAFKGS INKPEWMMLE
ALPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLQELNAPDI IIRNEKRMLQ
EAVDALLDNG RRGKTFTGPN KRPLRSLSDM LKGKQGRFRQ NLLGKRVDYS GRSVITVGPT
LRLHQCGLPK KMALELFKPF VYNKLEEKGL ATTIKQAKRL VDQETVEVWD ILADVVKEHP
VLLNRAPTLH RLGIQAFEPV LHEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSVESQVEA
RVLMMSTNNI LSPANGKPII NPSQDIVLGM YWLTRMRPGA KGSGKAFSSV QEAQYAFETG
LVDLQAVCKV RINGTLQETT VGRAILSDIV PKEVPFNEVN VTMGKKQIAA LIDKTFRLAG
AKATCILADK IMEYGFKYST AAGMSIGIDD MVIPAAKAPM IADAEKQVTE IQQQYDEGLI
TDGERYNKVV DIWAQTADKI AKEGMNAIEK QTFNVNGKEV VGPSFNPIYI MADSGARGSA
AQIRQLGGMR GLMAKPSGEI IETPITANFR EGLTVIQYFI STHGARKGLA DTALKTANSG
YLTRRLVDVA QDVVVSEIDC GVEDGLEITP IYEAGEIVQN IGDRILGRTA LKDVVDAATN
EVVVRANQEI TENDVKIIEG RGIDKVDIRS ALICQSKRGV CVKCYGRDLS RGATVNLGET
VGIIAAQSIG EPGTQLTMRT FHLGGAASRA VEQSVHTSRY DGVVKLQNVH AVTNRNGKLT
VMNRNGSALV IDEAGREREN FKLVYGAVLN FKEGDKVAKG QTVAEWDPYS NPIIAEVSAK
IQYQDIEEGS TMQEQVDAVT GFATKVIMES KSSDVKPTVF LVDGAGKTLN LPGRDIPARY
LIPVGAQLLV ADQQEVHAGD VIAKMHREAS KTKDITGGLP RVAELFEARK PKEAAIISEI
DGYVTFGKDV KGKQRVIVTP EVGEQKEYLI PKGKHVAVRE GEYVRAGEAL MDGPTNPHDI
LAVLGAKALS AYLVDEIQEV YRLQGVGIND KHIEVIVRQM LRKVEIRDAG DSRFLAGEQV
ERYAYMEENE RINKEGGQPA TCSPLLLGIT KVSLSTDSWI SAASFQETTK VLTEAAINSR
TDHLRGLKEN IIMGRLIPAG TGLTSYKRWK VSVHEDDDIG FVALPGMTSS VQPQG
