RPOC_LACLA
ID RPOC_LACLA Reviewed; 1207 AA.
AC Q9CEN7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=LL1799;
GN ORFNames=L0138;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK05897.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK05897.1; ALT_INIT; Genomic_DNA.
DR PIR; G86849; G86849.
DR RefSeq; NP_267956.1; NC_002662.1.
DR RefSeq; WP_014570699.1; NC_002662.1.
DR AlphaFoldDB; Q9CEN7; -.
DR SMR; Q9CEN7; -.
DR STRING; 272623.L0138; -.
DR PaxDb; Q9CEN7; -.
DR EnsemblBacteria; AAK05897; AAK05897; L0138.
DR KEGG; lla:L0138; -.
DR PATRIC; fig|272623.7.peg.1926; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_9; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002196; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1207
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067748"
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 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 454
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"
SQ SEQUENCE 1207 AA; 134731 MW; 636FA97EA4CAAA8B CRC64;
MVDVNKFESM RIGIASPQKI RYWSFGEVKK PETINYRTQK PEREGLFDER IFGPQKDWEC
ACGKLKGVFY KNQVCELCGV QVTTAKSRRE RMGHIELAAP ISHIWYFKGI PSRMGLALDM
SPRALEEVIY FASYVVIDPK ETDLEKKQLL TEREYREQLL KNGFGSFVAK MGAEAIQDLL
NDVDIDKEVS ELKEELKTVT GQRRVKIIRR LDVLSAFRKS GNALSWMVLN VLPVIPPDLR
PMVQLDGGRF ATSDLNDLYR RVINRNNRLK RLMELNAPNI IVQNEKRMLQ EAVDTLIDNG
RRGRPITGAG NRPLKSLSHM LKGKQGRFRQ NLLGKRVDYS GRSVIAVGPT LKMYQCGVPR
EMAIELFKPF VMAQLVKKEL AANIRAAKRK VERQDSDVWD VLETVVKEHP VLLNRAPTLH
RLGIQAFEPV LIDGKAIRLH PLACEAYNAD FDGDQMAIHL PLSEEAQAEA RLLMLAAEHI
LNPKDGKPVV TPSQDMVLGN YYLTMEEKGR EGEGMIFATP EEVEIAMRNG YVHLHTRIGI
ATKSLNKPWT ENQKDKILVT TVGKVIFNSI IPEGMPYLNE PTDVNLTTST DDRFFMDAGQ
DIKEVLAGID TVRPFKKGYL GNIIAEVFKR YRTTATSEYL DRLKNLGYHQ STLAGLTVGI
ADIPVVEDKH KIIDAAHKRV EQITKQFRRG LITDDERYNA VTGVWRDAKE ALEKRLIDEQ
DLTNPIVMMM DSGARGNISN FSQLAGMRGL MAAPNGKIME LPIISNFREG LSVLEMFFST
HGARKGMTDT ALKTADSGYL TRRLVDVAQD VIIREDDCGT DRGLVISDIA TGKEMVEPLF
ERLVGRYTRK SVLHPETGEM IIADDTLISE DVARKIIDAG VKEVTIRSVF TCKTPHGVCK
HCYGINLATG DAVEVGEAVG TIAAQSIGEP GTQLTMRTFH TGGVASSSDI TQGLPRVQEI
FEARNPKGEA IITEVTGTVE SIVEDPATRT REITVKGKTD TRSYTVGMAD VLMVEEGEFI
HRGAPLIQGS IEPKHLLQVR DALSVETYLL GEVQKTYRSQ GVEIGDKHIE VMVRQMLRKV
RVMDNGSTDI LPGTLMDISD FEALNETALL NGEMPATGRP VLMGITKASL ETNSFLSAAS
FQETTRVLTD AAIRGKEDHL LGLKENVIIG KIIPAGTGMF RYRNIEPLAD LTNAPEVEEV
ETETVEN
