ID A3WF57_9SPHN Unreviewed; 1423 AA.
AC A3WF57;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN ORFNames=NAP1_11723 {ECO:0000313|EMBL:EAQ28262.1};
OS Erythrobacter sp. NAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28262.1, ECO:0000313|Proteomes:UP000002995};
RN [1] {ECO:0000313|EMBL:EAQ28262.1, ECO:0000313|Proteomes:UP000002995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28262.1,
RC ECO:0000313|Proteomes:UP000002995};
RX PubMed=21952547; DOI=10.1128/JB.05845-11;
RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA Falkowski P.G.;
RT "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT sp. Strain NAP1.";
RL J. Bacteriol. 193:5881-5882(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ28262.1}.
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DR EMBL; AAMW01000002; EAQ28262.1; -; Genomic_DNA.
DR RefSeq; WP_007165468.1; NZ_CH672390.1.
DR STRING; 237727.NAP1_11723; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000002995; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 3.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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 NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01322};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000002995};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 236..515
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1384..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1423 AA; 157991 MW; 8FABA026754A1D93 CRC64;
MNELTKFTNQ LAKPETFDQI QIGIASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
IFGPVKDYEC LCGKYKRMKY KGVVCEKCGV EVTVTKVRRE RMGHIELAAP VAHIWYLKSL
PSRIGLLLDI QLKQLERILY FESYVVIEPG LTPLEKFQLL TEDELLEAQD EYGEDAFSAD
IGAEAVKVML MDLDLEQERE DLLEELATTK SALKPKKIIK RLKVVESFID SGNRPEWMIL
EVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIVRNEKRML
QEAVDALFDN GRRGRVITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVTGP
ELKLHQCGLP KKMALELFKP FIYARLDAKG LSMTLKQAKK WVEKERKEVW DILDEVIREH
PVLLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCSAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPANGKPI IVPSQDMVLG LYYLSMERQE KTPEYLENED GSKVEKLPRF
ADMAEVHHAL ETKAVTLHTK ILARVPQADE DGNIVMKRFE TTPGRMLIGE CLPKNHKVPY
DIINRLLTKK DIGDVIDEVY RHTGQKDTVL FADAIMVLGF RNAFKAGISF GKDDMIIPDA
KDPLVDETKS LVADYEQQYQ DGLITQQEKY NKVIDAWSRC GDQVADAMME EIKAQPIDDD
GKQAQINSIY MMSHSGARGS PAQMKQLAGM RGLMAKPSGE IIETPIISNF KEGLTVLEYF
NSTHGARKGL ADTALKTANS GYLTRRLVDV SQDCVIVEDD CKTENALEMR AIVQGGSVIA
SLGERILGRT VAEDIVNAAT DEVIVKAGTL VDEPMVKLIE EAEVQSAKIR SPLVCESDQG
VCATCYGRDL ARGTPVNIGE AVGVIAAQSI GEPGTQLTMR TFHIGGAAQL NETSHLESIS
DGKVELRDMP TITDKKGRIL SLARNGEIAV IDAEGREREM HKVPYGTVLH FKNGAKVKEG
DRLAEWDPFT LPIITEQSGV VRYQDLVEGT TLEEQTDDAT GIAQRVVTEN RATGRKKKEE
LRPRLMLQVE GQSEDDTEAQ RYMLAPGTTL SVEDGQQVEA GDILARASRE AAKTRDITGG
LPRVAELFEA RLPKDMSVIA KISGKIEFVR EYKAKRKIAI IPEEGDAVEY LIPKTKVIDV
QEGDFVKKGD TLISGSPNPH DILEVMGVEA LAEYLVNEIQ EVYRLQGVKI NDKHIEVIVR
QMLQKVEITN GGDTTLLPGE QVDLAEMLET NAKLGKGKQP AEGTPILLGI TKASLQTRSF
ISAASFQETT RVLTQASVEG KKDTLIGLKE NVIVGRLIPA GTGAGMNRMR VTASSRDAAL
KAQWKKQQEA LAAENASEPE PEADAVPSEE AMKAAMGGGD AAE
//