RPOC_MYXXD
ID RPOC_MYXXD Reviewed; 1403 AA.
AC Q1D7U2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MXAN_3078;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000113; ABF88775.1; -; Genomic_DNA.
DR RefSeq; WP_011553128.1; NC_008095.1.
DR AlphaFoldDB; Q1D7U2; -.
DR SMR; Q1D7U2; -.
DR STRING; 246197.MXAN_3078; -.
DR PRIDE; Q1D7U2; -.
DR EnsemblBacteria; ABF88775; ABF88775; MXAN_3078.
DR GeneID; 41360440; -.
DR KEGG; mxa:MXAN_3078; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002402; 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; -; 2.
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..1403
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308865"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 879
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1403 AA; 156314 MW; A31ADEAD93A3A3C2 CRC64;
MKDIFNFFEK PKDPLSFNAI RIALASPDKI RQWSHGEVKK PETINYRTFK PERDGLFCAR
IFGPVKDYEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RLGHITLATP VAHIWFLKSL
PSRIGNLLDI TLKELEKVLY CESYIVLDPK ATPLQKGELI SEDKMHRLYQ EHGEDSFTTG
MGGEAVREML KSLDVEKLSE ELRKDMRETT SEAKRKKYAK RLKVAEAFRV SGNKPEWMML
DVIPVIPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLQELNAPD IIIRNEKRML
QEAVDALFDN GRRGKTITGP NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELRLHQCGLP KIMALELFKP FIYNKLEEKG YVTTIKSAKK MVEKERPEVW DILEDVIREH
PVLLNRAPTL HRLGMQAFEP VLIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLSIEAQME
ARVLMMSTNN ILSPANGKPI IVPTQDMVLG IYYMTRAREF AGGEGRVFAS PDEVRAAYDH
GEVHLQAKVV CRIDGKRKET TVGRVLLWEV VPRAVGFDAI NKVLDKKSLG GLIDLCYRLT
GEKETVLLAD RVRSLGYYNA TRAGISIALK DMIIPAKKQE FLDFARKEVS EIENQYLEGL
ITDGERYNKV IDIWAEITEK VAQEMMQQIS QEETTGDRDG KRETRKQPSF NPIYIMADSG
ARGSAQQIRQ LAGMRGLMAK PSGEIIETPI TANFREGLSV LQYFISTHGA RKGLADTALK
TANSGYLTRR LVDVAQDAII NEYDCGTMDG LFIGALVEGG EIIEPLGERI LGRVALDDIL
DPVTGEVLVR ANEEIDEDRV RRIENSGMDK VKIRSVLTCQ AKRGICVECY GRDLARGRKV
SVGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AATRRAEQSS LENRYAGSVK FAGLVTVQKT
DGTLVAMNRN GEIVVVDDSG RERERYQVIY GARILVKEGQ RIEPGVLMAE WDPFAIPLLT
EVGGVVRYED IIEGVTMSEA LDEVTGLSRK TVIESKDPEA RPRVTIRDAN GNMMDLPSSR
NPASYFLPQG SIITVNDGDE IHPGEVIAKV PRETTKTKDI TGGLPRVAEL FEARKPKDAA
AIAEIDGVVS FGKDTKGKRK LIITPEVNGE QRTDLAKEYL ISKGKNISVH SGDRVKAGEA
MMDGSANPHD ILKVLGEKEL ARYLVDEVQE VYRLQGVKIN DKHIETIVRQ MLRRVRVTDV
GDTNFLVDEQ VEKWVFEEEN EKVMSEGKRP AVGEPLLLGI TKASLSTESF ISASSFQETT
KVLTEAAING KVDYLRGLKE NVIMGRLIPA GTGLPNYKHL DIAVESPTDE VNEMEAALAA
THGDTGPLGE PSRPVGTQTT GAA
