RPOC_LAWIP
ID RPOC_LAWIP Reviewed; 1388 AA.
AC Q1MPW9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=LI0904;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54958.1; -; Genomic_DNA.
DR RefSeq; WP_011526987.1; NC_008011.1.
DR AlphaFoldDB; Q1MPW9; -.
DR SMR; Q1MPW9; -.
DR STRING; 363253.LI0904; -.
DR PRIDE; Q1MPW9; -.
DR KEGG; lip:LI0904; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002430; 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; 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..1388
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308847"
FT BINDING 76
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 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1388 AA; 155137 MW; 435CA10239B2FFDF CRC64;
MSLDELFTVR STATANATQI RNLKAIQISI ASPENIREWS YGEVKKPETI NYRTFKPERD
GLFCAKIFGP VKDYECNCGK YKRMKHRGIV CEKCGVEVIA SKVRRERMGH IELAAPVAHI
WFLKTLPSKI GTLLDMAMAD LEKVLYFDSY IVLDPGSTNL TKMQVISEDQ YLQVIEHINE
ESFVVGMGAE AIRGLLEELN LETLRNSLRE ESQSTKSQTK KKKLTKRLKV VEAFIESGNR
PEWMIMEVIP VIPPELRPLV PLDGGRFATS DLNDLYRRVI NRNNRLKRLM ELGAPEIIIR
NEKRMLQEAV DALFDNGRRG RAIAGTNGRP LKSLSDMIKG KQGRFRQNLL GKRVDYSGRS
VIVVGPKLKL HQCGLPKKMA LELFKPFIYS ELEKRGHAST IKSAKKIVER EELVVWDILS
DVVREYPILL NRAPTLHRLG IQAFEPLLVE GKAIQLHPLV CAAYNADFDG DQMAVHIPLS
VEAQVECRVL MMSTNNILSP ANGSPVIVPS QDIVLGLYYM TVERSFEKGE GMVFCAPWEV
ISAIDNNQVN IHAKIKVRME DGNIYNTTAG RILVWEGLPK GLKFEYVNCV LTKKNIATLV
GNAYRDAGIK ATVILCDRLK DIGYEYATRA GITIGVKDLI IPATKKTIID TATSEVDDIE
RQYRDGIITR TEKYNKVVDV WTKATQDISS EMTKEISTEV VKDPKTERTE VNQSFNPIFM
MSNSGARGNQ DQMRQLAGMR GLMAKPSGEI IETPITSNFR EGLTVLQYFT STHGARKGLA
DTALKTANSG YLTRRLVDVV QDVIVYKNDC GTVDGIEVKQ VQDGGEIKQN LSERILGRVL
LYPIYHPVTN EIIFPENTLI DEYVVKKLEE IGIASVTIRS ALTCQSERGV CALCYGRDLA
RGHLVNIGET VGIIAAQSIG EPGTQLTMRT FHIGGTASRE IERSNFEALH SGRIVLTRVK
SVENRDGVHL VIGKSGQLSI VDEQGRERER YSLPNGARLY VKEGQEVTKG TFLAEWDPFN
EPFVSEVNGF IKFTDLIDGK TYQEKLDEAT HQSSMTIIEY RTTSFRPSIS ICDAEGQTKQ
RITSTTPAIY SLPAGAIIMV KDGQEVQAGD IIARKPRETS KTRDIVGGLP RVAELFEVRK
PKDMAVVSEI AGIVTYAGES KGKRKLIVTP EIGDPKEYLI PKGKHINVSD GDFVEAGDLL
TEGHPELHDI LKTRGEKYLA AYLVDEIQEV YRFQGVGIDD KHIEVIVRQM LRKITVTNPG
GTTFLVGEQV DKGDFKEENQ KIVEEGLEPA TAEPLVLGIT QASLTTSSFI SAASFQETTK
VLTEASLKGK MDYLRGLKEN VIVGRLIPAG TGYREYMELD IVVPEQKERP NKFLEELEER
PVLIEIDS
