RPOC_CELJU
ID RPOC_CELJU Reviewed; 1407 AA.
AC B3PK31;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 71.
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=CJA_0693;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(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=ACE85437.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; CP000934; ACE85437.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041551957.1; NC_010995.1.
DR AlphaFoldDB; B3PK31; -.
DR SMR; B3PK31; -.
DR STRING; 498211.CJA_0693; -.
DR PRIDE; B3PK31; -.
DR EnsemblBacteria; ACE85437; ACE85437; CJA_0693.
DR KEGG; cja:CJA_0693; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001036; 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..1407
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353321"
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 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1407 AA; 155406 MW; 47846B674E4B4780 CRC64;
MKDLLNLLKS QGQVEEFDSI RISLASPEMI RSWSFGEVKK PETINYRTFK PEREGLFCAK
IFGPVKDYEC LCGKYKRMKH RGIICEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
PSRIGLLLDM TLRDIERVLY FESYVVTEPG MTTLERGQLL TDEQYFEAME EFGDEFEAQM
GAEAIQTLMR AIDLETEVQR LREEIPNTSS ETKIKKYSKR LKLLEAFHFS GNKPEWMVME
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLNAPDI IVRNEKRMLQ
EAVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPT
LRLHQCGLPK KMALELFKPF IFSKLELRGL ATTIKAAKKM VEREEAVVWD ILDEVIREHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCSAYNAD FDGDQMAVHV PLTIEAQLEA
RALMMSTNNI LSPASGEPII VPSQDVVLGL YWMTRERINA KGEGMVFADT MEVSRAYYSK
QVDLQARIKV RLTETLIGAE GERTSETKLV QTTVGRVLLW EIVPAGIPLE MINRPMVKKA
ISAVINYCYR VVGLKATVIF ADRLMYMGYD FSTKSGSSIG VNDFTIPAAK ADIIARADAE
VKEIETQYAS GLVTQGEKYN KVIDIWSRAN DLVAKSMMEG ISKETVINRD GVEEQQSSFN
SVFMYADSGA RGSPAQIRQL AGMRGLMARP DGSIIETPIK ANFREGLNVL QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVT LQDCGTDSGL TMSPVIEGGD VIESLGDRIL
GRVVARDVIR PGSDEILVPA GTMIDEAWVG RIEEMGIDEV LVRSPITCES RNGICSMCYG
RDLARGHRVN PGEAVGVIAA QSIGEPGTQL TMRTFHIGGA ASRASAADSV QVKQEGTVRL
LNVKVVSNPA GNLVAVSRSG ELAIADASGR ERERYKIPYG ALITVKDGET VKGGQIVAKW
DPHTHPIVSE VAGTVAFSGM EEGLSIRRQT DELTGLSSIE ILDPAERPSA GKDLRPAITL
VDAKGKELFL ANTNVPAHYM LPAKAILTIN NGDIINVGDI VARIPQEGSK TRDITGGLPR
VADLFEARRP KEPAILAEIS GTVSFGKETK GKRRLIITPT DGQVLDDGST HYEVLIPKHR
QLTVFEGEMV AKGEVVSDGP ANPHDILRLQ GVEALARYIT NEIQDVYRLQ GVKINDKHIE
TIVRQMLRKV EITTMGDSSF VKGEQVELTS VLEENEKLRA EGKQPAHYER LLLGITKASL
ATESFISAAS FQETTRVLTE AAVTGKKDNL RGLKENVVVG RLIPAGTGLA YHNDRKRRRE
EALSEQVGVS AEDVEAALTE ALKSSVS
