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RPOC_STAA8
ID   RPOC_STAA8              Reviewed;        1207 AA.
AC   Q2G0N5; P47770; P77942;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 99.
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};
GN   OrderedLocusNames=SAOUHSC_00525;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-155 AND 1019-1140.
RX   PubMed=1402788; DOI=10.1099/00221287-138-9-1875;
RA   Aboshkiwa M.A., Coleman G., Rowland G.C.;
RT   "Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and
RT   rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits
RT   beta and beta'.";
RL   J. Gen. Microbiol. 138:1875-1880(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-555.
RX   PubMed=7772603; DOI=10.1016/0167-4781(95)00054-k;
RA   Aboshkiwa M.A., Rowland G., Coleman G.;
RT   "Nucleotide sequence of the Staphylococcus aureus RNA polymerase rpoB gene
RT   and comparison of its predicted amino acid sequence with those of other
RT   bacteria.";
RL   Biochim. Biophys. Acta 1262:73-78(1995).
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   -!- MISCELLANEOUS: The sequence of residues 1057-1140 was published in Fig.
CC       2 (PubMed:1402788) but not submitted to EMBL.
CC       {ECO:0000305|PubMed:1402788}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD29673.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD29673.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X64172; CAA45513.1; -; Genomic_DNA.
DR   PIR; S59956; S59956.
DR   RefSeq; YP_499097.1; NC_007795.1.
DR   AlphaFoldDB; Q2G0N5; -.
DR   SMR; Q2G0N5; -.
DR   STRING; 1280.SAXN108_0597; -.
DR   EnsemblBacteria; ABD29673; ABD29673; SAOUHSC_00525.
DR   GeneID; 3920378; -.
DR   KEGG; sao:SAOUHSC_00525; -.
DR   PATRIC; fig|93061.5.peg.471; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_9; -.
DR   Proteomes; UP000008816; 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.
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..1207
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000248949"
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         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         822
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         906
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1207 AA;  135409 MW;  8E87587E6C454003 CRC64;
     MIDVNNFHYM KIGLASPEKI RSWSFGEVKK PETINYRTLK PEKDGLFCER IFGPTKDWEC
     SCGKYKRVRY KGMVCDRCGV EVTKSKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLLLDM
     SPRALEEVIY FASYVVVDPG PTGLEKKTLL SEAEFRDYYD KYPGQFVAKM GAEGIKDLLE
     EIDLDEELKL LRDELESATG QRLTRAIKRL EVVESFRNSG NKPSWMILDV LPIIPPEIRP
     MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPGII VQNEKRMLQE AVDALIDNGR
     RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIAVGPSL KMYQCGLPKE
     MALELFKPFV MKELVQREIA TNIKNAKSKI ERMDDEVWDV LEEVIREHPV LLNRAPTLHR
     LGIQAFEPTL VEGRAIRLHP LVTTAYNADF DGDQMAVHVP LSKEAQAEAR MLMLAAQNIL
     NPKDGKPVVT PSQDMVLGNY YLTLERKDAV NTGAIFNNTN EVLKAYANGF VHLHTRIGVH
     ASSFNNPTFT EEQNKKILAT SVGKIIFNEI IPDSFAYINE PTQENLERKT PNRYFIDPTT
     LGEGGLKEYF ENEELIEPFN KKFLGNIIAE VFNRFSITDT SMMLDRMKDL GFKFSSKAGI
     TVGVADIVVL PDKQQILDEH EKLVDRITKQ FNRGLITEEE RYNAVVEIWT DAKDQIQGEL
     MQSLDKTNPI FMMSDSGARG NASNFTQLAG MRGLMAAPSG KIIELPITSS FREGLTVLEY
     FISTHGARKG LADTALKTAD SGYLTRRLVD VAQDVIVREE DCGTDRGLLV SDIKEGTEMI
     EPFIERIEGR YSKETIRHPE TDEIIIRPDE LITPEIAKKI TDAGIEQMYI RSAFTCNARH
     GVCEKCYGKN LATGEKVEVG EAVGTIAAQS IGEPGTQLTM RTFHTGGVAG SDITQGLPRI
     QEIFEARNPK GQAVITEIEG VVEDIKLAKD RQQEIVVKGA NETRSYLASG TSRIIVEIGQ
     PVQRGEVLTE GSIEPKNYLS VAGLNATESY LLKEVQKVYR MQGVEIDDKH VEVMVRQMLR
     KVRIIEAGDT KLLPGSLVDI HNFTDANREA FKHRKRPATA KPVLLGITKA SLETESFLSA
     ASFQETTRVL TDAAIKGKRD DLLGLKENVI IGKLIPAGTG MRRYSDVKYE KTAKPVAEVE
     SQTEVTE
 
 
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