RPOC_STAAU
ID RPOC_STAAU Reviewed; 1057 AA.
AC P0C1T4; P47770; P77942;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
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};
DE Flags: Fragment;
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RA Morse R., Collins M.D., Balsdon J.T., Reading S., Richardson P.T.;
RT "Cloning part of the rpoC gene encoding the B' subunit of the DNA-dependent
RT RNA polymerase from some Gram-positive bacteria and comparative amino acid
RT sequence.";
RL Submitted (AUG-1996) 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; X89233; CAA61517.1; -; Genomic_DNA.
DR PIR; T10908; T10908.
DR AlphaFoldDB; P0C1T4; -.
DR SMR; P0C1T4; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..>1057
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067798"
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"
FT NON_TER 1057
SQ SEQUENCE 1057 AA; 118612 MW; C7CB1260CD4BFFDA 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
MAQLDGGRFA 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 PNRNFIDPTT
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 LLKEVQK
