ID   RPOC_ZYMMO              Reviewed;        1391 AA.
AC   Q5NPK4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=ZMO0732;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [2]
RP   SEQUENCE REVISION TO 708-714.
RX   PubMed=19816441; DOI=10.1038/nbt1009-893;
RA   Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA   Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA   Chang Y.J., Samatova N.F., Brown S.D.;
RT   "Improved genome annotation for Zymomonas mobilis.";
RL   Nat. Biotechnol. 27:893-894(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008692; AAV89356.2; -; Genomic_DNA.
DR   RefSeq; WP_011240615.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q5NPK4; -.
DR   SMR; Q5NPK4; -.
DR   STRING; 264203.ZMO0732; -.
DR   PRIDE; Q5NPK4; -.
DR   EnsemblBacteria; AAV89356; AAV89356; ZMO0732.
DR   GeneID; 58026552; -.
DR   KEGG; zmo:ZMO0732; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001173; 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..1391
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225589"
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         809
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         889
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         892
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1391 AA;  154075 MW;  0784F023188B1026 CRC64;
     MNELANFANP LASTEHFDHI QISLASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
     IFGPIKDYEC LCGKYKRMKY KGIVCEKCGV EVTVSKVRRE RMGHIELAAP VAHIWFLKSL
     PSRIGLLLDM QLKQLERVLY FESYIVIEPG LTPLKKFQLL TEDELLEAQD QYGEDSFSAG
     IGAEAVKKLL EALDLETERE DLLEELKHTK SELKPKKIIK RLKVVESFIE SGNRPEWMIL
     EVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLMDLRAPD IIVRNEKRML
     QEAVDALFDN GRRGRTITGG NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVITTGP
     ELKLHQCGLP KKMALELFKP FIYSRLDAKG LSMTLKQAKK WVEKERKEVW DILEEVIREH
     PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCSAFNA DFDGDQMAVH VPLSLEAQLE
     ARVLMMSTNN ILSPANGKPI IVPSQDMVLG IYYLSMLKEN EPGEGMRLSN MTEVHQALNV
     GAVTLHSKII SRVPQVNEQG ETYMKRVETT PGRMLLGETL PQNYKVPFET INRLLTKKDI
     ADVIDTVYRH TGQKDTVLFA DAIMSLGFKY ACKAGISFGK DDMIVPAAKE ALVEETRALV
     QDFEQQYQDG LITQQEKYNK VIDAWSRCGD RVAGEMMKEI QMVHKGPDGR ELPVNAIYMM
     AHSGARGSAA QIKQLAGMRG LMAKPSGEII ETPIISNFKE GLTVLEYFNS THGARKGLAD
     TALKTANSGY LTRRLVDVSQ DCVVVEDDCG TERALEMKAI TQGGNVIASL GERILGRTLA
     EDIMGTDGQV AIPIGTLLDE AHIAVIEKIG IQSVKIRSPL VCESHGGVCA ACYGRDLARG
     TPVNIGEAVG VIAAQSIGEP GTQLTMRTFH IGGAAQLNEQ SHLEAVTDGR LQFRDLRTII
     DPQGKQIALS RTGEVVLVGT DGRELASSRI LLGAHLLHND GDMVKKGDRL AEWDPFTIPV
     ITESAGIVKY QDLVENQTLT EQVDEATGIS QRVVIEYRAP RGKEDLRPRL TLMNGDSGET
     ARYMLSPGTV ISVDDGQEVL AGTVLARVSR ESAKTRDITG GLPRVAELFE ARKPKENAII
     AKVSGRVEFG KDYKAKRKVI IRPDDGSEPI EYLVPKSKVI DAQEGDHVKR GDNLISGSPD
     PHDILEVLGV EALAEYLVSE IQEVYRLQGV KINDKHIETI VRQMLLKVEI THAGDSIFLP
     GEQVEKEDFE AVNAKLESQG QEPAQATPIL LGITKASLQT RSFISAASFQ ETTRVLTEAA
     VQGKIDTLSG LKENVIVGRL IPAGTGAAMK RLRVTANSRD AALRAANKAV NFEQPTIAIE
     SDNTDTPDAA E