ID F3YTX3_DESAF Unreviewed; 1385 AA.
AC F3YTX3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=Desaf_0221 {ECO:0000313|EMBL:EGJ48579.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ48579.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ48579.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ48579.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(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|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; CP003221; EGJ48579.1; -; Genomic_DNA.
DR RefSeq; WP_014258443.1; NC_016629.1.
DR STRING; 690850.Desaf_0221; -.
DR KEGG; daf:Desaf_0221; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR Proteomes; UP000007844; 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:UP000007844};
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; 154582 MW; BDB31EA68141D314 CRC64;
MTLDDLFAFR QTSATSIPAQ GIKAMKISIA SPEKIREWSF GEVKKPETIN YRTFKPERDG
LFCAKIFGPV KDYECNCGKY KRMKHRGIVC EKCGVEVIAS KVRRERMGHI ELAAPVAHIW
FLKTLPSKIG TLLDMTMADL EKVLYFDSYV VMDPRDTNLS KYQVISEDQY LQVIDHYGEE
AISVGMGAEA VRALLEELDL EKMRVELREE SQTTKSQTKK KKLTKRLKIV EAFSDSGNKP
EWMIMEVVPV IPPELRPLVP LDGGRFATSD LNDLYRRVIN RNNRLKRLLE LGAPDIIIRN
EKRMLQEAVD ALFDNGRRGR AITGTNGRPL KSLSDMIKGK QGRFRQNLLG KRVDYSGRSV
IVVGPKLKLH QCGLPKKMAL ELFKPFIYSK LEERGYASTI KSAKKMVERE ELVVWDILEE
VVREYPIMLN RAPTLHRLGI QSFEPLLVEG KAIRLHPLVC SAYNADFDGD QMAVHVPLSV
EAQIECRVLM MSTNNILSPS NGSPIINPSQ DIVLGLYYLT VERSFSRGEG KIFADQMEVI
AAVDNEVVDL HSRIKVRIDG KLHDTTPGRV IVSEILPAEM TFEMGNVVLN KKNIARLVSE
AYRTSGIKAT VILCDRLKDM GYEYATRAGV TIGVKDLSIP AKKAPLLQAS HDEVDDIERQ
YQEGIITRTE KYNKVVDVWT KCTNDVAKEM MREISIDILV DPKTGKKEAN SSFNPIYMMV
TSGARGNQDQ MRQLAGMRGL MAKPSGEIIE TPITSCFREG LSVLQYFNST HGARKGLADT
ALKTANSGYL TRRLVDVVQD VIISEIDCGT VDGLEVSHLI KGGDIKQKLS ERVLGRVTMF
DIYDDEKGEL IIPANTVIDE QVALKIDDAA LNSMTIRSGL TCASSHGVCA MCYGRDLARG
RLVNVGETVG IIAAQSIGEP GTQLTMRTFH IGGTASREIE RSSVESGHNG RAVLHRVKTV
KNAEGNWMVL NKSGQLSIVD EQGREREKYL LPSGAKLFVE SESLIKKGQM LAEWDPFNEP
FVSDVEGTVR FSDIVEGKTY QEKMDEATKR TTQTIIEYRS TNFKPAISIV DEEGRVKVRP
DSMVNATFQL PVGAIIMIRD GDFVKAGDII ARKPRETSKT KDIVGGLPRV AELFEVRKPK
DLAVVSEIDG VVSFGPDTKG KRKIIVTPET GDSKEYLIPK GKHITVSEGD FVESGELLTE
GYPELHDILK IKGEKVLARY LVEEIQDVYR FQGVSIDDKH IEIIVRQMLK KVSVTDPGDT
TFLAGEQVDK HKFMEENQQC IADGRKAAVA EPLVLGITQA SLTTDSFISA ASFQETTKVL
TEASLQGKED ALRGLKENVI VGRLIPAGTG YRRYMEAEID VPDQAERPDK FLEELDEPLG
VADRE
//
