ID   RPOC_LEGPL              Reviewed;        1401 AA.
AC   Q5WZL8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=lpl0363;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(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; CR628337; CAH14594.1; -; Genomic_DNA.
DR   RefSeq; WP_011214622.1; NC_006369.1.
DR   AlphaFoldDB; Q5WZL8; -.
DR   SMR; Q5WZL8; -.
DR   EnsemblBacteria; CAH14594; CAH14594; lpl0363.
DR   KEGG; lpf:lpl0363; -.
DR   LegioList; lpl0363; -.
DR   HOGENOM; CLU_000524_3_1_6; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000002517; 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; 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; Transcription; Transferase; Zinc.
FT   CHAIN           1..1401
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225545"
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         808
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   1401 AA;  155723 MW;  DFD326186DCA35B9 CRC64;
     MSDLLGILKQ QGQSEEFDAI KIALASPELI RSWSYGEVKK PETINYRTFK PERDGLFCAK
     TFGPVKDYEC LCGKYKRLKH RGVICEKCGV ELALAKVRRE RMGHIELASP VAHIWFLKSL
     PSRIGLLLDM TLRDIERVLY FEAFVVVDPG MTELERGQLL NDEAYLDAME QYGDEFDARM
     GAEAIRDLLR QIDLEDEIRN LREELPTTNS ETKIKKITKR LKLLEAFYES GNKPEWMIMD
     VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLNAPDI IVRNEKRMLQ
     ESVDALLDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPT
     LKLHQCGLPK KMALELFKPF IFSKLEFRGL ATTIKAAKKM VEREESVVWD ILDDVIREHP
     ILLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAYNAD FDGDQMAVHV PLTLEAQLEA
     RSLMMSTNNI LSPASGEPII VPSQDVVLGL YYLTREKVNA LGEGKIYSSA QEAQNFYEAG
     HLDIHAKIKI RMPKEDGETG YHLVETTVGR AILAEILPKG MPFDYINRTM TKKVISKVID
     SCYRKFGLKE TVIFADQLMY TGFKYATRSG ASIGIEDMEI PDDKASIIEH ADNEVREIES
     QFRSGLVTNG ERYNKVIDIW SRTNELVAKS MMSKIATEEV ADAKGNKVRQ ESFNPIFMMA
     DSGARGSAAQ IRQLAGMRGL MAAPDGSIIE TPITANFREG LNVFQYFIST HGARKGLADT
     ALKTANSGYL TRRLVDVAQD VVITEDDCGT DTGILMQPLI EGGDIVEPLH ERVLGRVVAS
     DVYIPTQTEP VVKAGTLLDE EWVEKLEKHG VDQVMVRSPI TCQTRFGLCA KCYGRDLARG
     HLVNTGEAVG IIAAQSIGEP GTQLTMRTFH IGGAASRATA ANNIQIKTKG VIRLHNIKTV
     THENKNLVAV SRSGEVTIVD EFGRERERYK VPYGAVISAQ DNSPVEAGQV IATWDPHTHP
     VISEVSGRLK FVDLIDGITM NRQTDELTGL SNIVIIDAKQ RSAAGRDLRP MVKLVTDEGD
     DIYLAGTNVP AQYYLPVDAI VNFEDRSLVG IGDVIARIPQ ERSKTRDITG GLPRVADLFE
     ARKPKDSAVM AEVSGLVNFG KETKGKRRLI INVSEDQCHE ELIPKWRHIS VFEGEHVERG
     EIIAEGALNP HDILRLLGVG ALANYIVNEV QDVYRLQGVK INDKHIEVIV RQMLRKRVIT
     FAGDSKFLVG EQVEESAMLQ ENDKLLAEGK QIARGTPILL GITKASLATE SFISAASFQE
     TTRVLTEAAV SGKVDELRGL KENVMVGRLI PAGTGYTYHQ SRKAKRARVA AGGDSSATHT
     VTASDVEHAL SEALNADNHE H