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RPOC_MYCLE
ID   RPOC_MYCLE              Reviewed;        1316 AA.
AC   P30761;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 126.
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=ML1890;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8446028; DOI=10.1111/j.1365-2958.1993.tb01112.x;
RA   Honore N.T., Bergh S., Chanteau S., Doucet-Populaire F., Eiglmeier K.,
RA   Garnier T., Georges C., Launois P., Limpaiboon T., Newton S., Niang K.,
RA   del Portillo P., Ramesh G.R., Reddi P., Ridel P.R., Sittisombut N.,
RA   Wu-Hunter S., Cole S.T.;
RT   "Nucleotide sequence of the first cosmid from the Mycobacterium leprae
RT   genome project: structure and function of the Rif-Str regions.";
RL   Mol. Microbiol. 7:207-214(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z14314; CAA78669.1; -; Genomic_DNA.
DR   EMBL; AL583923; CAC30844.1; -; Genomic_DNA.
DR   PIR; D87145; D87145.
DR   PIR; S31146; S31146.
DR   RefSeq; NP_302272.1; NC_002677.1.
DR   RefSeq; WP_010908593.1; NC_002677.1.
DR   AlphaFoldDB; P30761; -.
DR   SMR; P30761; -.
DR   STRING; 272631.ML1890; -.
DR   EnsemblBacteria; CAC30844; CAC30844; CAC30844.
DR   KEGG; mle:ML1890; -.
DR   PATRIC; fig|272631.5.peg.3580; -.
DR   Leproma; ML1890; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_11; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000000806; 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; 1.
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..1316
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067760"
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         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         537
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         891
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         968
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         975
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         978
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   CONFLICT        598
FT                   /note="A -> R (in Ref. 1; CAA78669)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1316 AA;  146896 MW;  7131AE63E53F6BCF CRC64;
     MLDVNFFDEL RIGLATAEDI RQWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPTRDWEC
     YCGKYKRVRF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
     APKDLEKIIY FAAYVITTVD EEMRHNELST LEAEMMVERK SVEDQRDADL EARAQKLEAD
     LAALEAEGAK ADARRKFRDG GEREMRQLRE RAQRELDRLE DIWSTFTKLA PKQLIVDENL
     YRELVDRYGE YFTGAMGAES IQKLMQDFDI EAEAESLREV IRNGKGQKKL RALKRLKVVA
     AFQQSGNSPM GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLIDL
     GAPDIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
     RVDYSGRSVI VVGPQLKLHQ CGLPKLMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERQR
     PQVWDVLEEV IAEHPVLLNR APTLHRLGIQ AFEPMLVEGK AIQLHPLVCE AFNADFDGDQ
     MAVHLPLSAE AQAEARILML SSNNILSPAS GRPLAMPRLD MVTGLYYLTT AVDGDTGAYR
     PAAEDRPESG VYSSPAEAIM AADRGVLSVR AKIKVQLTQV RPPADIEARW FGANGWRPGD
     PWIADTTLGR VMFNELLPLG YPFVNKQMHK KVQAAIINDL AERYPMIVVA QTVDKLKDAG
     FYWATRSGVT VSMADVLVPP RKKEILDHYE ERADKVEKQF QRGALNHDER NEALVEIWKE
     ATDEVGQALR DHYPVDNPII TIVDSGATGN FTQTRALAGM KGLVTNPKGE FIPRPVKSSF
     REGLTVLEYF INTHGARKGL ADTALRTADS GYLTRRLVDV SQDVIVREHD CQTERGIVVE
     LAVRVPDGSL IRELYIETSA YARTLGANAV DEAGNVIVAR GEDLGDPEID ALLAAGITQV
     KVRSVLTCTT GTGVCATCYG RSMATGKLVD IGEAVGIVAA QSIGEPGTQL TMRTFHQGGV
     GEDITGGLPR VQELFEARVP RGKAPIADVT GRVRLEDGER FYKITIVPDD GGEEVVYDKL
     SKRQRLRVFK HADGSERVLS DGDYVEVGQQ LMEGSADPHE VLRVQGPREV QIHLVREVQE
     VYRAQGVSIH DKHIEVIVRQ MLRRVTIIDS GSTEFLPGSL IDRAEFESEN RRVVAESGEP
     AAGRPVLMGI TKASLATDSW LSAASFQETT RVLTDAAINC RSDKLNGLKE NVIIGKLIPA
     GTGINRYRNI QVQPTEEARA SAYTIPSYED QYYSPDFGQA TGAAVPLDDY GYSDYR
 
 
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