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Database: UniProt
Entry: I0IMT1_LEPFC
LinkDB: I0IMT1_LEPFC
Original site: I0IMT1_LEPFC 
ID   I0IMT1_LEPFC            Unreviewed;      1583 AA.
AC   I0IMT1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   OrderedLocusNames=LFE_0876 {ECO:0000313|EMBL:BAM06580.1};
OS   Leptospirillum ferrooxidans (strain C2-3).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM06580.1, ECO:0000313|Proteomes:UP000007382};
RN   [1] {ECO:0000313|EMBL:BAM06580.1, ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|EMBL:BAM06580.1,
RC   ECO:0000313|Proteomes:UP000007382};
RX   PubMed=22815442; DOI=10.1128/JB.00696-12;
RA   Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT   Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT   Japan.";
RL   J. Bacteriol. 194:4122-4123(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA   Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "The complete genome sequence of the pioneer microbe on fresh volcanic
RT   deposit, Leptospirillum ferrooxidans strain C2-3.";
RL   Submitted (MAR-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|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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: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}.
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DR   EMBL; AP012342; BAM06580.1; -; Genomic_DNA.
DR   RefSeq; WP_014449071.1; NC_017094.1.
DR   STRING; 1162668.LFE_0876; -.
DR   GeneID; 78148675; -.
DR   KEGG; lfc:LFE_0876; -.
DR   PATRIC; fig|1162668.3.peg.1016; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000007382; 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; 2.
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; 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   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:UP000007382};
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          436..717
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          261..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         663
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         665
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         667
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1013
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1095
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         1105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1583 AA;  177089 MW;  CD3653DD79F8D922 CRC64;
     MNNSSFNENE KNQMVQFDKG NAGFQFDQEE QSFDDNSGHQ HPTSLYRDQD VLSFGAIKIM
     LASPERIKSW SFGEVKKPET INYRSFKPER DGLFCAKIFG PVKDWECNCG KYKRMKHRGV
     ICDKCGVEVI QSKVRRERMG HIELASPVAH IWFLKGLPSR IGNLLDMTIK DLDQILYFEA
     YVVTELGDIL TQMDSNRNNL VRNLLVKNHK SIYRVSSEQG VFEKIDESLT DEFLTNHETS
     PFIAIQDRDL SLFEEWGNVA SDSNEKPKTR KSKPKLNSEG LPAPLKPKFR NPLTLDLYSE
     ETSEVITRAG LKLPETSLKG EVYLVILDEE TLQVVNKAIS SNEKRREELE QDFKKHRPIP
     KEDFEKIKRE FPRANFKGEI GAEAIRTLLR GLKLEELSVE MHIQMADPMV SSAAKKKIAK
     RQKIVEAFRK SGNKPEWMIL DVIPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL
     KRLLDVSSPT PQLIIHNEIR MLQEAVDALF DNGRRGRVIR GANRRPLKSL SDMLKGKQGR
     FRQNLLGKRV DYSGRSVIVI GPELKLSQCG LPKKMALELF KPFIFQKLEE RGLVSNIKTA
     KRRVEKEDPI VWDILDEVIQ EHPVLLNRAP TLHRLGIQAF DPVLVEGKAI RLHPLVCAAF
     NADFDGDQMA VHVPLSVEAQ LEARVLMMSV NNILSPANGK PIMVPTQDMV LGCYYLSKER
     KGAKGEGANF SSAHEVRIAY DANVVEPHAR ITVRISSEKY GKKRIETTVG RVLFSEILPK
     DIAFEEINRE LTKKVLTNLI DQCYRRVGRQ ETVVFLDRIK QIGFEFATKS GISIAIDDMK
     IPGNKSKAIE VANSEVLEIE NQYNEGLITA GERYNKVIDK WAQVTEQVAD EMMEELKAEE
     LSVQNGISLG RGTDPVRFNS IYMMADSGAR GSAQQIRQLG GMRGLMAKPS GEIIETPITA
     NFREGLNVLQ YFISTHGARK GLADTALKTA NSGYLTRRLV DVAQDVIITE EDCGTVHGIE
     VSALVEGGET IEPLEERILG RVASEDISST YGMVGSKKKG QEVLVAAGEE INEEKIEKIK
     EAGIDIVRIR SVLTCQAKRG VCAACYGRDL SRGKRVELGE AIGIIAAQSI GEPGTQLTMR
     TFHIGGTAQV AKQSVHESKR DGVVRYENLV TVKNKEGSQI AMSKNGKLVI IGKDGREKER
     YSIVYGARVQ VEDGATVTLG SKLVEWDPFT TPILTEVTGQ VLFRDIQDRL TMREEIDETS
     GLKSRVIIDN SKQNMRPRIE IRETGSKIRK EYPLPIGAHI LVEEKDIVSP GDVVAKIPRE
     STKTKDITGG LPRVAELFEA RKPKEQAIIT EIEGVVEFKE GRQGRGNRII IVKNDQGEER
     EYIIPKGKHI SVHENDWVEA GEPLMDGSVN PHDILNVLGP QDLMTYLVNE VQEVYRLQGV
     SINDKHIEVI VRQMLRKTRI DDPGDTEFLV GSHVDRGQFD AVNSEMISIG KKPANGSAML
     LGITKAALST ESFVSAASFQ ETTRVLTEAA INGKTDDLAG LKENVIVGRL IPAGTGFPKF
     RMTAIANSDA EVGNGDIYEK VSP
//
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