ID   RPOC_LISIN              Reviewed;        1201 AA.
AC   P77879;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 3.
DT   03-AUG-2022, entry version 132.
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=lin0286;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1053.
RC   STRAIN=ATCC 33090 / DSM 20649 / NCTC 11288 / Serovar 6a;
RA   Morse R., Collins M.D., Balsdon J.T., Reading S., Richardson P.T.;
RT   "Cloning part of the rpoC gene encoding the B' subunit of the DNA-dependent
RT   RNA polymerase from some Gram-positive bacteria and comparative amino acid
RT   sequence.";
RL   Submitted (AUG-1996) 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; AL596164; CAC95519.1; -; Genomic_DNA.
DR   EMBL; X89229; CAA61513.1; -; Genomic_DNA.
DR   PIR; AG1468; AG1468.
DR   PIR; T09641; T09641.
DR   RefSeq; WP_010990309.1; NC_003212.1.
DR   AlphaFoldDB; P77879; -.
DR   SMR; P77879; -.
DR   STRING; 272626.lin0286; -.
DR   PRIDE; P77879; -.
DR   EnsemblBacteria; CAC95519; CAC95519; CAC95519.
DR   KEGG; lin:rpoC; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_9; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000002513; 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; 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..1201
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067754"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         818
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"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         902
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   CONFLICT        774
FT                   /note="L -> S (in Ref. 2; CAA61513)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1201 AA;  134755 MW;  52876C3776033DBF CRC64;
     MLDVNNFEYM KIGLASPDKI RSWSHGEVKK PETINYRTLK PERDGLFCER IFGPMKDWEC
     SCGKYKRVRY KGVVCDRCGV EVTKSKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVMDM
     SPRALEEIIY FASYVVTEPG DTPLEKKQLL SEREYRVYRE KYGKGFSAGM GAEAIKKILA
     DIDLEKETND LKEELKSAQG QRRTRAIRRL EVMEAFRNSG NNPSWMVLDV LPVIPPEIRP
     MVQLEGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPNII VQNEKRMLQE AVDALIDNGR
     RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPNL KMYQCGLPKE
     MALELFKPFV MKELVGRGLA HNIKSAKRKI ERMAPEIWDV LEEVIREHPV LLNRAPTLHR
     LGIQAFEPTL VEGRAIRLHP LVCTAYNADF DGDQMAVHVP LSAEAQAEAR ILMLAAQNIL
     NPKDGKPVVT PSQDMVLGNY YLTLERENAV GEGTIFKDIN EAQLAYQNGY VHLHSRIAVF
     AGSIPNERFT DEQRKQLLIT TVGKLIFNTI LPKSFPYINE PTKFNLEIET PAKYFVDTTT
     DVRAHIAAQE LIDPFKKKIL GNIIAEVFKK FHITETSKML DRMKDLGFKI STKAGMTVGI
     ADILTLEEKH EILEKAHDTV EKITKSFRRG LITDDERYER VIGVWNAAKD EIQGKLILSL
     DRLNPIFMMQ DSGARGNISN FTQLAGMRGL MADPSGRIVE LPITSNFREG LTVLEYFIST
     HGARKGLTDT ALKTADSGYL TRRLVDVAQD VIIREDDCGT DRGLTIKAIR EGTEIIEPLE
     ERLEGRYSRK TIRHPETKEV IARENDLITE AIATQIVDAG IEEVTIRSAF TCNTKHGVCK
     KCYGKNLATG TEVEVGEAVG IIAAQSIGEP GTQLTMRTFH TGGVAGDDIT QGLPRIQEIF
     EARNPKGQAI ITEVGGEVVS IEEGRDRQQE ITIQGTDDRR SYNIPYTARL RVEEGSIVER
     GEALTEGSVD PKALIRVRDV LSVQEYLLAE VQKVYRMQGV EIGDKHVEVM VRQMLRKIRV
     MDTGDTNILP GTLMDIHTFT EANRDAILSG SQPATGRPVL LGITKASLET DSFLSAASFQ
     ETTRVLTDAA IKGKRDELLG LKENVILGKL VPAGTGIGRY RKLKSEVIKE TAEVTDEITN
     I