ID C8X481_DESRD Unreviewed; 1385 AA.
AC C8X481;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 OrderedLocusNames=Dret_2071 {ECO:0000313|EMBL:ACV69355.1};
OS Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 /
OS HR100).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfohalobiaceae; Desulfohalobium.
OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV69355.1, ECO:0000313|Proteomes:UP000001052};
RN [1] {ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Desulfohalobium retbaense DSM 5692.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV69355.1, ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV69355.1,
RC ECO:0000313|Proteomes:UP000001052};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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|HAMAP-Rule:MF_01322,
CC 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}.
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DR EMBL; CP001734; ACV69355.1; -; Genomic_DNA.
DR RefSeq; WP_015752497.1; NC_013223.1.
DR STRING; 485915.Dret_2071; -.
DR KEGG; drt:Dret_2071; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000001052; 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: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; 2.
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:UP000001052};
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 241..520
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1385 AA; 153813 MW; C95045ED8BFC2ECB CRC64;
MTLDDLFTMR GAGSSQSQSE ELKGIQISLA SPEKIREWSY GEVKKPETIN YRTFKPERDG
LFCAKIFGPV KDYECNCGKY KRMKHRGIVC EKCGVEVIPS KVRRDRMGHI ELAAPVAHIW
FLKSMPSKIA TLLDMTMAEL EKVLYFDSYI VLDPGQTNLK KQQTLSEDQY LQIVEHYGED
ALRVGMGAEA AKELLEEIEL ESLRHTLKEE SLATRSQTKR KKLAKRLKVV EAFIESGNHP
AWMILEVVPI IPPELRPLVP LDGGRFATSD LNDLYRRVIN RNNRLKRLLE LGAPDIIIRN
EKRMLQEAVD ALLDNGRRGR AITGTNGRPL KSLSDMIKGK QGRFRQNLLG KRVDYSGRSV
IVVGPKLKLH QCGLPKKMAL ELFKPFIYSK LESLGHASTI KSAKKMVERE DVVVWDILED
VVKEYPILLN RAPTLHRLGF QGFEPLLVEG KAIQLHPLVC AAYNADFDGD QMAVHVPLSV
QAQIESRVLM MSTNNILSPA NGAPIIVPSQ DIVLGLYYLS LARSFERGEG KIFADAEEVI
MALDAQAITL HARIKVRIDG ELIDTTPGRI LLKGILPEKV PFSLVNSILN KKAIGRLVGE
AYRLAGTKAT VLLCDRLKDM GYEYATQAGV TIGVKDLLIP EQKKPLLEKA RAEVDSIESQ
YRDGIITRTE KYNKVVDVWT KATNDVSSEM MRDISVDRIS DAHGERVEEN PSLNPIFMMS
NSGSRGNVDQ MRQLAGMRGL MARPSGEIIE TPITSSFREG LTVLEYFTST HGARKGLADT
ALKTANSGYL TRRLVDVVQD VIVGELDCGT VDGIEISHLM RGGEMQTRLS ERILGRMTLF
DVTNPETGEV VVPADSIIDE EYARRIDDAG INSVMIRSVL TCNSEKGVCA KCYGRDLARG
HLVNVGESVG IIAAQSIGEP GTQLTMRTFH IGGTASKEIE QSSITAQHKG RIVLNRVRTV
SNSDGMHMVL GKSGQIGVVD EQGLEREKYV LPPGARLYIQ PGDEVSKGTL LAEWDPFNEP
FVTDVDGVVS FADIEEGKTY QTKVDEATQR TTKTIIEYRS TNFRPSISIC DEKGEVKTRP
ESSLAATFQL PVGAILMVED GQQVQAGDVI ARKPRETSKT KDIVGGLPRV AELFEVRKPK
EMGVVTEIDG VVSFGPDSRG KRKIIVTPDT GDPREYLIPK GKHITVQEGD FVEAGELLTE
GNHELHDLLR VKGEKYLANY LVEEVQDVYR FQGVHINDKH IEIIVRQMLK KVNITDPGDS
SLLVGEQVEK TRFMEENQKV LKRGGQPAVA EPLVLGITQA SLTTESFVSA ASFQETTKVL
TEAALQGKKD FLQGLKENVI VGRIVPAGTG FRPYLQAGIK VPNQPERSER FLEDLEDEQR
YNGVG
//
