RPOC_METC4
ID RPOC_METC4 Reviewed; 1405 AA.
AC B7KN46;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Mchl_4387;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-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_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; CP001298; ACK85163.1; -; Genomic_DNA.
DR RefSeq; WP_012255172.1; NC_011757.1.
DR AlphaFoldDB; B7KN46; -.
DR SMR; B7KN46; -.
DR PRIDE; B7KN46; -.
DR EnsemblBacteria; ACK85163; ACK85163; Mchl_4387.
DR KEGG; mch:Mchl_4387; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR BioCyc; MEXT440085:MCHL_RS21330-MON; -.
DR Proteomes; UP000002385; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1405
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165843"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1405 AA; 154860 MW; 1AD790FCE45C7497 CRC64;
MNQEVMNLFN QQAQPQSFDQ IKISISSPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRMK YKGVICEKCG VEVTLARVRR DRMGHIELAA PVAHIWFLKS
LPSRIGLLLD MALKDLERIL YFESYVVIEP GLTPLKERQL LSEEEYLRAQ EEYGEDSFTA
MIGAEAIRRI LMELDLEGIA TSLKEEIATT TSELKPKKLM KRLKIIEAFQ LSGNKPEWMI
LTVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP DIIIRNEKRM
LQEAVDALFD NGRRGRVITG ANKRPLKSLA DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
PELKLHQCGL PKKMALELFK PFIYARLDAK GFSATVKQAK KLVEKEKPEV WDILDEVIRE
HPVMLNRAPT LHRLGIQAFE PKLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQL
EARVLMMSTN NILHPANGQP IIVPSQDIVL GLYYLSIVAD GSVGEHKADD KNNPMQGVFG
DIGQLEHALA AKSVSLHSKI KWRWRGLGPD GEPVSRIYDT TPGRVILSGV LPMHPKVPFD
VVNKLMTKKE ISAMIDTVYR HCGQKESVIF CDRIMALGFS HAFKAGISFG KDDMVVPENK
WSIVEDTRTL VKDYEQQYND GLITQGEKYN KVVDAWAKCS DKLAAEMMGR ISAVQKDENG
ADKQVNSIYM MSHSGARGSP AQMKQLAAMR GLMAKPSGEI IETPIISNFK EGLDVLEYFN
STHGARKGLA DTALKTANSG YLTRRLVDVA QDAVIREVDC GTTNGIKMRA IIDAGQVVAP
LSIRILGRAT AEDLVAQDGT VIVKTNETIE ERHLPAINAA GIQEVKIRSV LVCQTKSGVC
ATCYGRDLAR GTPVNMGEAV GVIAAQSIGE PGTQLTMRTF HIGGAAQIAD SSFVESSFEG
TIKIRNRSLA KNSDGDLIAT GRSVAVVIVG PDGTERAVHR LQYGARVRVD EGDTIKRGQR
IAEWDPYTRP IVAEVDGIVG YEDLYDGQSI TETTDESTGI AKRVVIDWRG SSRTSDLKPA
MLVLDQDGKP VKLARGSDAR YYLPVDAIIG LDPGAKVRAG DVLARVSTDS AKTRDITGGL
PRVAELFEAR RPKDAAIIAE KSGSIAFGRD YKNKRRLTLT PHDGSDAVEY LIPKGKHIHL
QDGDVVELGD YIVDGNPAPH DILAIKGVEE LAAYLVNEIQ EVYRLQGVSI NDKHIEVIVR
QMLQKVEITD GGDSDILTGD QIDRTELADF NEKLLAEGKK PIQGVPVLLG ITKASLQTKS
FISAASFQET TRVLTEAAVN GKVDTLDGLK ENVIVGSLIP AGTGSLAADI RSIARRRDNL
ILQQRSAENA ANAAELSELP PAAAE
