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Database: UniProt
Entry: RPOC_ROSS1
LinkDB: RPOC_ROSS1
Original site: RPOC_ROSS1 
ID   RPOC_ROSS1              Reviewed;        1504 AA.
AC   A5USR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
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=RoseRS_1264;
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) 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: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; CP000686; ABQ89669.1; -; Genomic_DNA.
DR   RefSeq; WP_011956021.1; NC_009523.1.
DR   AlphaFoldDB; A5USR6; -.
DR   SMR; A5USR6; -.
DR   STRING; 357808.RoseRS_1264; -.
DR   KEGG; rrs:RoseRS_1264; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000006554; 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; -; 2.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; 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; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1504
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_1000086411"
FT   REGION          265..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1468..1504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1468..1487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         626
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         628
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         630
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1002
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1075
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1082
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         1085
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1504 AA;  169331 MW;  F29B6580F639D851 CRC64;
     MLEINDFSAI RISLASPEDI LSWSHGEVTK PETINYRTLK PERDGLFCER IFGPTKDWEC
     YCGKYKRVRY KGVVCDKCGV EVTRSKVRRE RMGHISLASP VSHIWFVKGT PSRLGLLLDI
     SPRNLERVLY FASYMIVHVD EELKAQAREA LQAEYREKRE RIQQEAESKQ IELSTQLTQD
     LGGMESAQIT TQRRIEEEYR RLRDEISAEA ERLRSDLEEK QGEAAEEDIL FRGTVLIEEG
     EIITEKTLDA LDELLDQELE TLEQRKQRDL EDAEQLTGAE RERKEYEASQ ERERLQERLQ
     SELDRLVREE KERLEQIDSI KLKRILSEQE YRALREIAPG VFRADMGAGA VRDMIVRTID
     LDKLAEELQN EVYTTQGQRR KKATKRLRVV EAFRKSGNRP EWMILTVLPV IPPDLRPMVQ
     LDGGRFATSD LNDLYRRVIN RNNRLKRLME LNAPEIIVRN EKRMLQEAVD ALIDNGRRGR
     AVSGKGKHRL KSLSDMLKGK QGRFRQNLLG KRVDYSGRSV IVVGPDLKLH QCGLPKKMAL
     ELFKPFVMRR LVEKGFAHNI KSAKRIVERV RPEVWDVLEE VIKDYLVLLN RAPSLHRLSI
     QAFEAKLIEG SAIQLHPLVC AAFNADFDGD QMAVHVPLSR KAQEEARMRM LSKYNLLSPA
     TGDPIITPSQ DIVLGCYYLT MVKDGAKGSG KMFASIDEAL LAYDKGLIDI QAPIFVRMTG
     TVYGESDRPV RMLSPDENGA PRMLLETTIG RIIFNNELLE PLRFRNRLIA KKGLREIIAD
     CYKYYTNLNN LTEADLDTIR AMYGDRPRDD LARYFGSEMT ASQADRIKTL GFRYATRGGM
     TIGVDDIEIP PKKQDILAEA EKRVTEVERQ FRRGLITEEE RYREIVEIWQ NATKQTTEAV
     KQHLNPFGPV AMMVNSAARG NINQLSQMAG MRGLMSDPTG RIIELPIKSN FREGLSVLEY
     FVSTHGGRKG LADTALRTAD AGYLTRRLID VAQDNIVTID DCGTDEGLWI YRADDREVLQ
     DFEQRILGRL LAAPLVDPRT GEILANRNDE IDEALVRKCK ELAIDAVYVR SPLACKADYG
     ICRMCYGRNL ATGKLVDIGE AVGIIAAQSI GEPGTQLTLR TFHTGGVASA DDITQGLPRV
     QEIFEARTPK GKAILAEIDG IVELVREDEV RKIRVVATEL YTDDHELPPH YEPVVADGAQ
     VNEGDVLAQS NRADLNGEPI VARIAGVVRI GAGQISVINE EREVREVVAP HTARLAPGIE
     NGARVVAGQH LTEGSADPQE LLALQGREAV QRYLVNEAQK VYRSQGVDIN DKHIEVIVRQ
     MLRRVRIEEP GDTDYLPGEL IDSTEFVRKN AEIISQGGEP ATASTMLLGI TKASLTTDSF
     LAAASFQETT RVLTEAAITG KVDYLRGLKE NVVIGKLIPA GTGIEKRRQL AEEIIGELAN
     VAPATSTAVV EQERPDREAD EALRRRLRAL IGGDGDDGER NNGDFDDQVG EDVVIPPDDD
     DQEA
//
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