RPOC_FINM2
ID RPOC_FINM2 Reviewed; 1202 AA.
AC B0S2E5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=FMG_1117;
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAG08535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP008971; BAG08535.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041250604.1; NC_010376.1.
DR AlphaFoldDB; B0S2E5; -.
DR SMR; B0S2E5; -.
DR STRING; 334413.FMG_1117; -.
DR PRIDE; B0S2E5; -.
DR EnsemblBacteria; BAG08535; BAG08535; FMG_1117.
DR KEGG; fma:FMG_1117; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_0_9; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001319; 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..1202
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353365"
FT REGION 301..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1202
FT /note="Disordered"
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 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 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 793
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 867
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1202 AA; 135074 MW; 144947ACB5DB3275 CRC64;
MVQKNTFEAM KIGLASPDKI RQWSWGEVKK PETINYRTLK PEKEGLFCEK IFGPTKDYEC
NCGKYKRIRY KGIVCEKCGV EVTKSKVRRE RMGHIELATP VSHIWYFKGI PSRMGLLLDM
SPRALEKVLY FASFVVIDPG KTDLYEKQLL TEQEYEEYCD KYEEDVDFRA KMGAEAIKEL
LQKIDLQEEY KNLTETFEGS TGQKKVRILR RLEVVEAFIE SKNDPSWMIM DVIPVIPPDI
RPMVQLEGGR FATSDLNDLY RRVINRNNRL KRLLDIGSPE IIVRNEKRML QEAVDALIDN
GRRGKPVTGP GNRPLKSLSD MLKGKSGRFR QNLLGKRVDY SGRSVIVIGP NLKFYQCGLP
KKMALELFKP FVIRELVKRE ISHNVKNAKK LVERENDKVW DVLEDIIVDH PVLLNRAPTL
HRLGIQAFEP ILVEGKAIKL HPLVCTAYNA DFDGDQMAVH LPLSPEAQAE ARLLMLSTNN
ILAPKDGKPI TTPSQDMVLG SFYMTTRKEG QKGEGLIFKD IDEMMLAYAM HYVTLQTIVK
VRRNSVNNDG TSKIVESTVG RFIFNEGIPQ DLGMVNRNED PYSLEVDLQV DKKMLSKIID
LTFRRYGNIR TAELLDYIKS MGYKYSTIGA LTISMGDITI PDSKKGIIEQ AEQRIDMVQD
IYLQGDITNE ERYKKVIEIW EQCIKDVTRA LMTNLPADNN LNIMAVSGAR GSENQIRQLG
GMRGLMSDTA GNTIEIPITS NFREGLSVQE FFISTHGSRK GLSDTALRTA DSGYLTRRLV
DVSQDVIITE DDCGTDEYIV AKEIKDGNRQ VEDLKSRIIG RYAFEDILDL DTGEIIVHKN
DMINEAIAER IESKGIKEVK VRSVLGCKMK HGVCAKCYGR NLATGKPVNI GEAVGIIAAQ
SIGEPGTQLT MRTFHSGGIA GVGITSGLPR VEELFEARKP KGLAYITEIE GTVKIQENKK
RNDVIVTSED GEEQVYQIPY GAHIRVNEGD HVEKGEPLTE GSINPQDILR VNGAEGVRDY
IIREVQKVYR LQGVDIDDKH IEIIIRQMMS KIKVEESGDS GFLSGSVVDA RDFKMTNEQL
IKEGKTPATG THSLMGITKA SLATESFLSA ASFQETTRVL TETSIKGKVD HLIGLKENVI
IGKLIPAGTG IAKYDRIEVD YDGKAEDDMI EAEKAQASND SEEAEESTII SGNYESLQDE
DK
