RPOC_LEUCK
ID RPOC_LEUCK Reviewed; 1220 AA.
AC B1MVW7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=LCK_01547;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC organisms. {ECO:0000305};
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; DQ489736; ACA83371.1; -; Genomic_DNA.
DR RefSeq; WP_012305432.1; NC_010471.1.
DR AlphaFoldDB; B1MVW7; -.
DR SMR; B1MVW7; -.
DR STRING; 349519.LCK_01547; -.
DR PRIDE; B1MVW7; -.
DR EnsemblBacteria; ACA83371; ACA83371; LCK_01547.
DR KEGG; lci:LCK_01547; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_9; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002166; 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; 2.
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..1220
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353387"
FT REGION 1197..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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"
SQ SEQUENCE 1220 AA; 135411 MW; 5F849DBEFC6E6C07 CRC64;
MAIDVNKFES MQIGLASPDK IRSWSYGEVK KPETINYRTL KPEKDGLFDE RIFGPTKDYE
CACGKYKRIR YKGIVCDRCG VEVTSSKVRR ERMGHIELAA PVTHIWYFKG IPSRMGLVLD
MSPRSLEEII YFASYVVIEP GDAPVEKKQL MTEREYRELK REYGASFKAG MGAEAIKDLL
ASVDLAAEAD QLKRELQEAT GQKRVRAVRR LDIIEAFLQS DNKPQWMVMD VIPVIPPDLR
PMVQLEGGRF ATSDLNDLYR RVINRNNRLK RLLDLNAPGI IVQNEKRMLQ EAVDALIDNG
RRGRPVAGPG NRPLKSLSHM LKGKQGRFRQ NLLGKRVDYS GRSVIDVGPF LKMNQMGLPR
PMAIELFRPF IMKELTTRKL AGNVKSAKRK IDKADEDVMD VLEDVIKEHP VLLNRAPTLH
RLGIQAFEPV LVSGKAMRLH PLVTEAYNAD FDGDQMAIHV PLSDEAQAEA RLLMLAAGHI
LAPKDGKPIV APSQDMVIGN YYLTTEEAGR EGEGMIFSSV EEAKIAFASK VVHYHTRIGI
QTSSFPEAKP FTDEQRSKIM VTSVGKLIFN EILPVDFPYI NEPSEDNFKG ISDQFFIEPG
EDIHDYLADT AVIGAFKKGF LSDVIAEVYK RYKVTETSLL LDRMKDLGYE KSTESGLTVS
MNDVTELTEK PAILEDAHKQ VATVTKQFRR GLITDSERYQ RVTEIWTKAK DVIQDKLIAS
FEPTNPIFMM QDSGARGNIS NFVQLAGMRG LMAGPGGKII ELPVTANFRE GLTVMEMFIS
THGARKGMSD TALKTANSGY LTRRLVDVAQ DVIVREWNNN ADRGVAVKAI MDGTSVVEPL
YDRILGRYAM KSVFNPETGD KLVSRNEMID EDVAKAIVAA GIEEVTIRSV FTSTTEHGVS
VLDYGRNLAT GEEVEVGEAV GTVAAQSIGE PGTQLTMRNF HTGGVAGGND ITQGLPRVQE
IVEARIPKGR AEISEVTGTV VAIEENPAER TKAVTIEGET DTRTYTLPLA ARMRFAEGDD
IQRGDAINEG PIDPKELLAV TDTLTTESYM LTEIQKVYRL QGIEVSDKHI EVMIRQMLRK
VRVMDPGETS LLPGMLMDIA DFQRANEPAL FDGLVPATAR PVLLGITKAA LETNSFLSAA
SFQETTRVLT DAAIRGKNDP LVGLKENVII GKIIPAGTGM AEYRKIKSKV VGEVVAQPEV
EQEPTPDIPK LDDVAKSFEE
