RPOC_SYNAS
ID RPOC_SYNAS Reviewed; 1381 AA.
AC Q2LQ86;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SYNAS_02940;
GN ORFNames=SYN_00063;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC76173.1; -; Genomic_DNA.
DR RefSeq; WP_011416207.1; NC_007759.1.
DR AlphaFoldDB; Q2LQ86; -.
DR SMR; Q2LQ86; -.
DR STRING; 56780.SYN_00063; -.
DR PRIDE; Q2LQ86; -.
DR EnsemblBacteria; ABC76173; ABC76173; SYN_00063.
DR KEGG; sat:SYN_00063; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001933; 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; -; 2.
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; 1.
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..1381
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240827"
FT REGION 1362..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1381 AA; 153997 MW; 8FCD824BEC7D655D CRC64;
MEDVFSYFEK PKDPIRFNAI KISIASPDKI LSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC LCGRYKRMKH RGVVCEKCGV EVIKSKVRRE RMGHITLATP VAHIWFLKSL
PSRIGNVLDL TLKELERILY FESWIVLDPR NTPLRKKDLL SDEEYNDLRE QYGPDGFQAG
IGAEAVRKLL EEVDLEGLDV ELRDELKTAS SDTKRKKVIK RLKVIEALRK SGNRPEWMIL
TVLPVIPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLQELNAPE IIIRNEKRML
QEAVDVLFDN GRRGRAITGT NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVITVGP
DLRLHQCGLP KKMALELFKP FVYNRLQEKG YVTTVKSAKK MVERETAEVW DALDEVVREY
PVMLNRAPTL HRLGLQAFEP VLIEGKAIQL HPLVCTAFNA DFDGDQMAVH VPLSIEAQTE
ARVLMMSTNN ILSPANGKPI IIPSQDVVLG IYYLTRSKED VLGHGMSFSN PEEVRSAFDA
GAVELRARIK VRIDDELKET TVGRVILYEI IPEAISFDVI NKVMNKKELA NLIDYCYRLC
GEKTTVILAD RLKDMGFKYA THSGMSFAVR NLNIPKNKKD IVVRADRDVL EIQKQYMDGL
ITDGERYNKV IDLWAQATEK IASEMMGGIE TEEQITTEGK KVVESFNPIY MMADSGARGS
NAQIRQLAGM RGLMAKPSGE IIETPITANF REGLTVLQYF ISTHGARKGL ADTALKTANS
GYLTRRLVDV AQDCIITQQD CGTVDGISVS ALMEGGEIIE TAGERVLGRV VLEDIMDPFT
GEVLVGANQE IDESLSEKID RAGIESVRIR SVLTCKAKYG VCARCYGRDL GHGHLVNIGE
AVGIIAAQSI GEPGTQLTMR TFHIGGTAKF EEHSTLDSRH DGIVKYVDLN YVVSKIGETV
VMSRHGEIHV LDEQLRSRGK YTVPYGAHLK VKDGQSVKRG DRMAEWDPFS IPILAEVDGT
VKFGDIIEGK TMQEQVDEVT GLSRKVIVEF KGADLRPRVS LKDATGKTAK VPGTNAAARH
LLSVGVNIVV SEGDQVKAGD IIAKIPRETT KTKDITGGLP RVAELFEARK PKDFAVISEI
DGVVSYGKDA KGKRKVIVTP EIGDEKEYLI PKGKHVSVQE GDRVIAGEAL MSGVNNPHDL
LMIKGEKALA RYLVDEVQEV YRLQGVKIND KHMEVIVRQM LRRVKVIDPG DTPFMADEQV
EKFRFQEENE KAIARGEQPA IGEPVLLGIT KASLSTQSFI SAASFQETTR VLTEASLAGK
VDYLRGLKEN VIMGRLIPAG TGLVMYRKLG IKTVADEDAE SVEIEGDENS NKKSLDMHAA
N
