RPOC_MAGSA
ID RPOC_MAGSA Reviewed; 1496 AA.
AC Q2W2I2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=amb3139;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE51943.1; -; Genomic_DNA.
DR RefSeq; WP_011385505.1; NC_007626.1.
DR AlphaFoldDB; Q2W2I2; -.
DR SMR; Q2W2I2; -.
DR STRING; 342108.amb3139; -.
DR PRIDE; Q2W2I2; -.
DR EnsemblBacteria; BAE51943; BAE51943; amb3139.
DR KEGG; mag:amb3139; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000007058; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1496
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240807"
FT REGION 1467..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 989
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 992
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1496 AA; 165697 MW; E34633DE01B69D9C CRC64;
MNELMKIFGQ VSGTQSFDQI RISIASPERI RSWSYGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKY RGIICEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
PSRIGLLCDM TLKDLERILY FENYVVVEPG LTPLKIRELL TEEQYMRAVD EYGEDAFTAK
IGAEAIRDML TVIDLETEKA QLKVDLKETT SEAKRKKLVK RMKLVEAFME SGSRPEWMIL
EVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPE IIVRNEKRML
QEAVDALFDN GRRGRAITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELKLHQCGLP KKMALELFKP FVYSKLELYG MATTIKAAKR MVEKERPEVW DILEEVIREH
PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCTAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPANGKPI IVPSQDIVLG IYYITMERDE VPGQVLKIRS MDELKGAIAN
NAILFYCPTD PNTKIDTKDL DTLLDRLASR NVTAHRRVNP SSKDALEAGL KGGHLRLFNV
EKPGVPLVFA DVNDAEKAIK DGKAILFKVP VFVNMAEIEE ALTEKTITLH TKIRARFDTV
DSEGTPVTQI VDTTPGRMML SVILPKNKNV PFSLINRLLT KKEIQNVIDV VYRHCGQKET
VIFADRVMGL GYSNAFKAGI SFGKDDLVIP PEKETLVGET EEKAKEYEQQ YQDGLITQGE
KYNKVVDAWS KCTDDVADAM MKQISSLVPG KQINSIYMMA HSGARGSAAQ MKQLAGMRGL
MAKPSGEIIE TPIISNFKEG LTVLEYFNST HGARKGLADT ALKTANSGYL TRRLVDVAQD
AIICEEDCGT TNGLTVSPVI EGGEVIASLA ERILGRSAAR DIVNPLTGEV IVKAAQMIQE
TEVELIDAAG IETVVIRSVL TCDSEEGVCG SCYGRDLARG TRVNVGEAVG VIAAQSIGEP
GTQLTMRTFH IGGAAQRGAE QSSIEATFDG TVQVINRNVV VNSSGASIVM SRNCEVALLD
INNRERARHR VPYGAKLLVD EAQKVTKGTK LAEWDPYTLP IITERAGVAH YVDLTEGLSM
REVVDEATGI ASKVVVDWKQ QPRGADLRPR VTLRDEKGEE LLLANGLEAR YFMSVDAILS
VENNTKVNAG DVLARIPRES SKTRDITGGL PRVAELFEAR KPKDHAIISD CDGRVEFGKD
YKSKRRILVV PEEGDAIEYL IPKGKHISVQ EGDYVRRGDP LMDGNPVPHD ILKVLGVEAL
AQYLINEIQE VYRLQGVKIN DKHIEVIVRQ MLQKVEITDP GDTTLLVGEQ VDRVEFDIEN
SKAIREQGRP ASGTPVLQGI TKASLQTHSF ISAASFQETT RVLTEAAVSG KVDSLQGLKE
NVIVGRLIPA GTGAVMNRLR AIAAKRDKDM QVEGESEVPA IPPVAEGSAP EAPPAE
