ID   RPOC_SINMW              Reviewed;        1401 AA.
AC   A6U852;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Smed_0979;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) 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; CP000738; ABR59832.1; -; Genomic_DNA.
DR   RefSeq; WP_011975167.1; NC_009636.1.
DR   RefSeq; YP_001326667.1; NC_009636.1.
DR   AlphaFoldDB; A6U852; -.
DR   SMR; A6U852; -.
DR   STRING; 366394.Smed_0979; -.
DR   EnsemblBacteria; ABR59832; ABR59832; Smed_0979.
DR   GeneID; 61614977; -.
DR   KEGG; smd:Smed_0979; -.
DR   PATRIC; fig|366394.8.peg.4099; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001108; 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..1401
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353437"
FT   REGION          1378..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         810
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"
FT   BINDING         891
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         894
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1401 AA;  155335 MW;  263F5170CD95E433 CRC64;
     MNQEVMNLFN PQVPAQTFDS IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
     RIFGPIKDYE CLCGKYKRMK YKGIICEKCG VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
     LPSRISTLLD MTLKDIERVL YFENYIVTEP GLTSLKENQL LSEEEYMIAV DEFGEDQFTA
     MIGAEAIYEM LASMNLEKIA GDLRSEMAET TSDLKQKKLM KRLKIVENFM ESGNRPEWMI
     MKVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP GIIIRNEKRM
     LQESVDALFD NGRRGRVITG ANKRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVTG
     PELKLHQCGL PKKMALELFK PFIYARLDAK GYSSTVKQAK KLVEKEKPEV WDILDEVIRE
     HPVLLNRAPT LHRLGIQAFE PILVEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLSLEAQL
     EARVLMMSTN NILHPANGAP IIVPSQDMVL GLYYLSIMNQ NEPGEGMAFS DMGELHHALE
     TKAVTLHAKI RGRYKTVDAE GNPVSKIYET TPGRMIIGEL LPKNPNVPFE TCNQEMTKKN
     ISKMIDTVYR HCGQKDTVIF CDRIMQLGFS HACRAGISFG KDDMVIPDTK VKIVGDTEAL
     VKEYEQQYND GLITQGEKYN KVVDAWGKAT EKVAEEMMAR IKAVEFDDSG RQKPMNSIYM
     MSHSGARGSP NQMRQLGGMR GLMAKPSGEI IETPIISNFK EGLTVNEYFN STHGARKGLA
     DTALKTANSG YLTRRLVDVA QDCIVTHTDC GTDKGLTMTA IVDAGQVVAS IGQRILGRTA
     LDNIDNPVTG ERIVDAGRMI LEPDVVAIEK AGIQSVRIRS ALTCEIQTGV CGVCYGRDLA
     RGTPVNMGEA VGVIAAQSIG EPGTQLTMRT FHLGGTATVV DQSFLEASYE GTVQIKNRNM
     LRNSDGVLVA MGRNMAIQIL DERGVERSSQ RVAYGSKIFV DDGDTVRRGQ RFAEWDPYTR
     PMMTEVEGTV HFEDVVDGIS VLESTDESTG ITKRQVIDWR STPRGTDLKP AIVIKDKNGN
     IAKLARGGEA RFMLSVDAIL SVEPGQKVSQ GDVLARSPLE SAKTKDITGG LPRVAELFEA
     RRPKDHAIIA EIDGTIRFGR DYKNKRRVMI EPAEDGVEPV EYLIPKGKPF HLQDGDYIEK
     GDYILDGNPA PHDILAIKGV EALASYLVNE IQEVYRLQGV VINDKHIEVI VRQMLQKVEI
     TDAGDSTYIV GDNVDRIELE DVNDSLIAEG KKPAFGDPVL LGITKASLQT PSFISAASFQ
     ETTKVLTEAA VAGKTDNLQG LKENVIVGRL IPAGTGGTMT QIRRIATARD ELILEERRKG
     TGAESATPML AAMANDPAAA E