RPOC_SULMW
ID RPOC_SULMW Reviewed; 1464 AA.
AC A8Z5T2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=SMGWSS_056;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS30483.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000770; ABS30483.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A8Z5T2; -.
DR SMR; A8Z5T2; -.
DR STRING; 444179.SMGWSS_056; -.
DR EnsemblBacteria; ABS30483; ABS30483; SMGWSS_056.
DR KEGG; smg:SMGWSS_056; -.
DR HOGENOM; CLU_000524_3_1_10; -.
DR Proteomes; UP000000781; 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; -; 2.
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; 2.
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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1464
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353443"
FT REGION 1143..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1221
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 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 838
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 922
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1464 AA; 167039 MW; AEE8DA2584CF8C91 CRC64;
MSKKQYKISH FMTTKISLRI SSPEEILKDS YGEIIKPETI NYRTNKPERN GLFCEKIFGP
IKDYECFCGK YKKKLYKEII RLRQLNKELK VKGLFCNRCG VEITKNTVRR TRMGHINLVV
PIVHIWGFRS TPNKIGSILG LSSQQLDMII YYERYVVIQP GIANSYNNLS IKKLDLLTEE
EYTYILNKIP IGNKYLYDND PNKFIAKMGA ECLEELLIRV DLEVLLSDLK KEIKNEESKQ
RKIELFKRLN VVECFIEGKK KGNKIESIIL KVLPVIPPEL RPLVPLDGGG YASSDLNDFY
RRILIRNNRL KRLIHISAPE IILRNEKRML QEAVDSLLDN SKKILAVKSE SNRPLKSLSD
SLKGKQGRFR QNLLGKRVDY SARSVIVVGP KLKLHECGLP KEIAAEIYKP FLIRKLLERK
IVRTVKSAKK LISKKDPIIW DILKYLLKGH PVLLNRAPTL HRLGIQSFQP KLIEGKAILL
HPLVCSAFNA DFDGDQMAVH LPLSNEAILE AKLLMLASQN ILNPANGYPI TVPSQDMVLG
LYYMTKELKS TYESKIKGEG MCFSSLEEVE IAYNNKVVEI HAIIKVKVKI LENIGLISKI
IKTTVGRVLF NIVVPPKVGY INKLLTNKSL RKIINYILYN TNIPTTAKFL DKIKDLGYYH
AFKGGLSFNL NDISIPKEKK SLVKRAIEKV SLVKDNYNLG LITNNERYNQ IIDIWTNTNV
SLTEKVINYM RKSKQGFNSV YMMLDSGARS SKEQIRQLSG MRGLMAKPQK TSSLGSEIIE
NPILSNFLEG LSILEYFIST HGARKGLADT ALKTADAGYL TRRLVDSAQD VIIQEDDCKT
LLGIKISAVK KKEKIIETLS SRVLGRIALN NIYDPTNNNV LIKSSQMIDE KNINLIEKAS
IDTIEVRSPL TCKSKTGICR KCYGRNLANG LMIQKGEAIG VIAAQSIGEP GTQLTLRTFH
VGGTAGNIYE YSKIKAKYDG IIEYEDIQVV KNLVISRSSE IRLLNNHKDK VILMKKKIPY
GAKLYVSNKQ LVKKNDIICS WDPYNAVIIA EFTGKIRYSN IERDEQTGFK VISERKTPTL
KIVNKKNEIL KSYNIPVGAH LVVNDGDIIN EGSILIKIPI KDLKSGDITG GLPRLSELFE
ARNDDDDDDY YDSDYYDYYD YSDDDDDYDD YDDYYYNYDD DENDNDNDYD YDYDYDYDYD
SDSHNSYSHN SYSPSSNDNY DYDYDSDSDY DSDYDYGDIS LNEILDIKGL RAAQKKLINE
IQEVYRSQGV KINDKHFEVI VRQMTQKVEI IKSGDTSFLE GNIEYTDVFL EENKRILNMK
FIEESGDSKK FFKGQLVNFH ELKKENYLLK LSNKNKILFR DVITAISKPI IQGITKAALQ
TKSFLSAASF QETTKVLYEA AISNKTDYLN GLKENVILGN KIPAGTGLKK SSYEEIIIGD
GNQKLKKKDS EINKKLKIEN KILK
