RPOC_GRAFK
ID RPOC_GRAFK Reviewed; 1433 AA.
AC A0M3Y8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=GFO_2369;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67333.1; -; Genomic_DNA.
DR RefSeq; WP_011710236.1; NC_008571.1.
DR AlphaFoldDB; A0M3Y8; -.
DR SMR; A0M3Y8; -.
DR STRING; 411154.GFO_2369; -.
DR PRIDE; A0M3Y8; -.
DR EnsemblBacteria; CAL67333; CAL67333; GFO_2369.
DR KEGG; gfo:GFO_2369; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000755; 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; -; 1.
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; 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 TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1433
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308836"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1433 AA; 160104 MW; C107812EF0BEBB3B CRC64;
MARNNDKNTV QRFNQISIGL ASPESILAES RGEVLKPETI NYRTHKPERD GLFCERIFGP
VKDYECACGK YKRIRYKGIV CDRCGVEVTE KKVRRDRVGH INLVVPVAHI WYFRSLPNKI
GYLLGLPSKK LDMIIYYERY VVIQAGNAKN EEGEPLKKMD FLTEEEYLNI LDELPQENQY
LDDSDPNKFI AKMGAECLIE ILKRIDLDEL SYELRHKANN ETSKQRKTEA LKRLQVVEAL
RDANKNRENN PEWMIMKVVP VIPPELRPLV PLDGGRFATS DLNDLYRRVI IRNNRLKRLM
EIKAPEVILR NEKRMLQESV DSLFDNTRKS SAVKTDSNRP LKSLSDSLKG KQGRFRQNLL
GKRVDYSARS VIVVGPELKM FECGLPKNMA AELYKPFIIR KLIERGIVKT VKSAKKIIDK
KEPVVWDILE NVLKGHPVLL NRAPTLHRLG IQAFQPKLIE GKAIQLHPLA CTAFNADFDG
DQMAVHLPLG PEAILEAQLL MLASHNILNP ANGSPITVPS QDMVLGLYYM TKHKKTTKDE
TVIGEGLTFY SAEELVIAYN QKRVDLNAGI KIRTKDYNEE GELVYMIKDT TVGRVLFNEA
VPEKAGYINE VLTKKSLREI IGKILKITSV PETSEFLDEI KGLGYGFAFR GGLSFSLGDI
IIPEEKQSMI DEANEQVEGI IGNYNMGLIT NNERYNQVID IWTSTNAGLT DLAMKRIRED
KQGFNSVYMM LDSGARGSKE QIRQLTGMRG LMAKPKKSNS GGGEIIENPI LSNFKEGLSI
LEYFISTHGA RKGLADTALK TADAGYLTRR LVDVSQDVIV NEDDCGTLRG VEVKPLKKNE
EIVESLGERI LGRISLNDVV NPSTQEHIVA TNEEITEEIV AKIEAAPIES VEVRSPLTCE
AKKGICIKCY GRNLATNKIV QTGEAVGVVA AQSIGEPGTQ LTLRTFHVGG IAGNISEDNK
LEAKFAGVAE IEDLKVVKGE APDGGTADIV ISRTAELKIK DKKTGVVLSN NNIPYGSQIN
INDGATVKEG EVICTWDPYN GVIISEFAGK IKYENVEQGV TYQVEIDEQT GFQEKVISES
RNKKLIPTLH ILGKKDEVIR SYNLPVGAHL MVDNEEKIGV GKILVKIPRK SSKAGDITGG
LPRVTELFEA RNPSNPAVVS EIDGVVSFGK IKRGNREIIV ESKLGEVKKY LVKLSNQILV
QENDYVRAGM PLSDGSITPE DILNIKGPNA VQQYLVNEVQ EVYRLQGVKI NDKHFEVVVR
QMMRKVRIVD PGDTIFLENQ LVHKADFIEE NNKLFGMKVI EDAGDSEKLK AGQIITPRDL
RDENSILRRE DKNLATARDV ITATANPVLQ GITRASLQTK SFISAASFQE TTKVLNEAAV
SGKIDYLEGL KENVIVGHRI PAGTGMRKYD SIIVGSKEEF DQMLEKKQEV NYN
