RPOC_SULNB
ID RPOC_SULNB Reviewed; 1509 AA.
AC A6Q6I3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SUN_0132;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(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}.
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DR EMBL; AP009179; BAF71092.1; -; Genomic_DNA.
DR RefSeq; WP_011979825.1; NC_009663.1.
DR AlphaFoldDB; A6Q6I3; -.
DR SMR; A6Q6I3; -.
DR STRING; 387093.SUN_0132; -.
DR EnsemblBacteria; BAF71092; BAF71092; SUN_0132.
DR KEGG; sun:SUN_0132; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006378; 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; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1509
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308893"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1509 AA; 166492 MW; 02F9A396A14D9D50 CRC64;
MSKFLENLTP IDLNSDDRPK DIAALQLKVA SPEKVLSWSY GEVKKPETIN YRTLKPERDG
LFCAKIFGPI RDYECLCGKY KKMRYKGVVC EKCGVEVTSS KVRRNRMGHI DLIAPVAHIW
YVSSLPSRIG TLLGVKMKDL ERVLYYEAYI VKTPGEASYD NEGLNPVQKY DVLNEEQYQQ
ISSRFGDTGL DARMGGEIVQ ELLADLDLVD MFAQLKEDIQ ATKSEAKRKT IVKRLKVIEA
FLHSGNRPEW MMLTQLPVLP PDLRPLVSLD GGKFAVSDVN DLYRRVINRN QRLKRLVELD
APEIIVRNEK RMLQEAVDAL FDNGRRGNAV KGANKRPLKS LSEVIKGKQG RFRQNLLGKR
VDFSGRSVIV VGPDLRMDQC GLPKKMAIEL FKPHLMAKLE EKGYATTLKQ AKKMIEQQVN
EVWECLEEVV ENYPVLLNRA PTLHKLSIQA FHPRLIEGKA IQLHPLVCSA FNADFDGDQM
AVHVPLSDEA IAEAKVLMLA SMNILLPASG KAIAVPSQDM ILGLYYLTLE KNDVKGQHKL
FANVEEVEIA FEQQALDLNA RIRTVLDGRI ATSTAGRLIL KSIIPDYVPE KYWNKVLKKK
DIGALVDYIY KIGGVSETAG FLDNLKDMGF KYATKVGVSI SVDDIKIPEM KEGRVQTAKE
QVKEIQRQYA AGLLTDQERY NKIIDIWTDA NNSIAEALMD LIRKDKDGFN SVHMMADSGA
RGSAAQIRQL SGMRGLMAKS DGSIIETPIT SNFREGLNVL EYFISTHGAR KGLADTALKT
ANAGYLTRKL IDVAQNVKVS MTDCGTHEGV EVSDIVVGNE MIEPLADRIY GRVLAEDIID
PITSEVLVSE GTMIDEETAT RVQEAGVRSV VMRAPSSCKA PKGICAKCYG LNMADNKMVK
RGEAVGVIAA QSIGEPGTQL TLRTFHTGGT ATAGKEERSV VATKEGFVRY YNLSVYRNTE
GKLIVANRRN AGVLLVEPKI KAVNKGKVSI VVTHDEIVIS VENNGDDEVR YNLRKSDVAK
SNELAGVAGK IEGKLFLPLK DGDMVEEGDS IVEVIKEGWS IPSRIPFASE LKVEDGAPVT
QEVLSEAKGT VKFFLLKGDY LEAHDGVKSG DKVEEKGLFA VVVDDNNREA GRHYISRGSV
VHVDNNAKVE RGATLSAPEK TTQVVIAEWD PYSEPIIAEQ KGTLKFEDII PGVTVVEQFD
EVTGDTRLEL NEYIPAAYKP AITLATESGE LIRYQLDPKT ILFVKDGEEV NIADILAKTP
KAAIKSKDIT GGLPRVSELF EARRPKDIAL IAQIDGVVSF GKPLRGKERL IISGDNGQIT
EQFIDKNKVA LVHTGEYVHA GEKLTDGIVS SHDILAALGE KALYDYIVSE VQMVYRRQGV
NISDKHIEIV TSQMMRQVKV VESGDSNFIA GDIISRRKFQ EENQRVIALG GEPAIAEPML
VGITRAAVGA DSIISAASFQ DTTKVLTSAS IAGTVDMLED LKENVVIGRL IPVGTGMIDS
DEIKFSAAE
