ID J9YZX4_9PROT Unreviewed; 1372 AA.
AC J9YZX4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HIMB59_00010070 {ECO:0000313|EMBL:AFS49194.1};
OS alpha proteobacterium HIMB59.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS49194.1, ECO:0000313|Proteomes:UP000006097};
RN [1] {ECO:0000313|EMBL:AFS49194.1, ECO:0000313|Proteomes:UP000006097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB59 {ECO:0000313|EMBL:AFS49194.1,
RC ECO:0000313|Proteomes:UP000006097};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (AUG-2012) 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: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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01322}.
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DR EMBL; CP003801; AFS49194.1; -; Genomic_DNA.
DR STRING; 744985.HIMB59_00010070; -.
DR KEGG; apc:HIMB59_00010070; -.
DR PATRIC; fig|744985.3.peg.999; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000006097; 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; 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 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:UP000006097};
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 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"
SQ SEQUENCE 1372 AA; 153288 MW; 3C22759D4E4013DF CRC64;
MKDLTNLFKN NNQTLNFDQI KISVSSPEQI RSWSFGEIKK PETINYRTFK PEREGLFCAR
IFGPTKDYEC LCGKYKRMKF KGITCEKCGV EVTLSKVRRE RMAHIELAAP VAHIWFLKSL
PSRIGLALDI TLKNLEKVLY FESHIVIDPL MSGLEQNQLL TDEELEEAIE QFGEDSFKHG
IGAEAVHEIL SSLDLEKEIE KLVEESAATS SETKKKKILK RMKVMEGFKK SNIKPEWMIL
KVLPVIPPEL RPLVPLEGGR FATSDLNDLY RRVINRNNRL KRLLDLRAPD IIVRNEKRML
QESVDALFDN GRRGRVITST NKRPLKSLSE MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELKLHQCGLP KKMALELFKP FIYNKLESYG FASTLKSARK MVESERPEVW DILDEVIREH
PILLNRAPTL HRLGIQAFEP ILIEGKAIQL HPLVCTAFNA DFDGDQMAVH IPLSLEAQLE
ARVLMMSTNN ILSPSSGKPI IVPSQDIVLG IYYLSLINDN EEVKKYFSHI GEVEFALENK
SINLHTPILF RTKTFNKETN EYEDKKFTTS PGRVLLFKTV PQSENLPFDC INKILTKKEI
SNLLDNVYRF TGQKATCIFV DQIMNVGFKY AAKAGISFGK DDLVIPEEKN SLIQETQKQV
NSLEAQYQEG LITEREKYNK VVGLWSTCTD KVAKAMMKTV STTKDNQINS VYIMAHSGAR
GSEAQLKQLA GMRGLMARPS GEIIENPITS NFKDGLTVLE YFNSTHGARK GLADTALKTA
SSGYLTRRLV DVAQDLTITQ KDCSCSNGLT VDTVYESGEV AIPLKDRVFG RYLADDVKTS
EGKVIMKNGE YISHEEIETI EKENITSVRI KSPITCGCVN GICAKAYGRD LAKGEPVNTG
EAVGIIAAQS IGEPGTQLTM RTFHVGGVAS SSAEKSNFES PSDGKIKIQN LRSVINQAGS
EIIINRTTEL EIYDLNNKLV STFRAPYGST LLVKDKAEVK LNDLLLEWDP YTVPIVAEES
GILDFSDLVE GVSFIEKFDE TTGISSKVII DWKSFQGKQD LKPQLVITDD KGNPVKSKGS
NNSSYDLSVG IVLNIEKGKE VKAGDIIARI PRASSKTKDI TGGLPRVADI FESRKPKNPA
VLAEVSGVIE FGKDIKSKRR IIINPEDGDP VEYLIPKGTY IYFNEGDKVN KGDMIVDGTP
APTDILNILG IEALAEYMVR EVQKVYRLQG VLIDDKHIEC ITRQMLQKVE VIESGDSEYL
VGDVLDRTTV LEKNIELKEA GKNEAKFKMM ILGITKASLQ TNSFISAASF QETTRVLTEA
AINGKVDKLT GLKENVIVGK LIPAGTGNVI RALRKEAKIR DNSLLKQIEN TK
//
