RPOC_CYTH3
ID RPOC_CYTH3 Reviewed; 1438 AA.
AC Q11QA6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=CHU_3168;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG60408.1; -; Genomic_DNA.
DR RefSeq; WP_011586517.1; NZ_FPJX01000011.1.
DR AlphaFoldDB; Q11QA6; -.
DR SMR; Q11QA6; -.
DR STRING; 269798.CHU_3168; -.
DR PRIDE; Q11QA6; -.
DR EnsemblBacteria; ABG60408; ABG60408; CHU_3168.
DR KEGG; chu:CHU_3168; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001822; 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..1438
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308831"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1438 AA; 160129 MW; 2DC97C2AE079081F CRC64;
MAFRKNKKLN NDFTKVTISL ASPESILEGS HGEVTQPETI NYRTYKPEMG GLFCERIFGP
VKDWECHCGK YKRIRYKGII CDRCGVEVTE KKVRRERMGH IELVVPVAHI WYFRSLPNKI
GYMLGLPTKK LDQIIYYERY VVIQSGVKSE DGINYLDFLT EDEYLDILDK LPRENQLLDD
KDPNKFIAKM GADALETLLS RLNLDELSYS LRHAAANDTS QQRKAEALKR LKVVEAFRDA
RSRIENKPEW MIIRMVPVIP PELRPLVPLD GGRFATSDLN DLYRRVIIRN NRLKRLIEIK
APEVILRNEK RMLQEAVDSL FDNSRKINAV RAEGNRALKS LSDMLKGKQG RFRQNLLGKR
VDYSGRSVIV VGPELKMHEC GLPKDMAAEL FKPFIIRKLI ERGIVKTVKS AKKIVDRKDP
VVWDILENVL KGHPILLNRA PTLHRLGIQA FQPKLIEGKA IQLHPLVCTA FNADFDGDQM
AVHVPLGHEA ILEASLLMIA SHNILNPANG APITVPSQDM VLGLYYVTKG RKSTPEHPIK
GEGMAFYGAE EVVIAINEGR LSQHAHIKVK GIVRTDAGEL VEQMIDTVAG RVLFNLVVPE
EVGFVNELLT KKKLQLIIGM VFKIAGMSKT AKFLDDIKQI GFQMAFRGGL SIGLDNIGIP
ADKNTLIDGA KKEVDSVWSN YLMGLITDNE RYNQVIDIWT RVNSEITDTL MKQLEADQQG
FNPIYMMMHS GARGSREQIR QLGGMRGLMA KPQKNLQGSV GEIIENPILS NFKEGLDVIE
YFISTHGARK GLADTALKTA DAGYLTRRLV DVAQDAIINE QDCGTLRGLT VSALKDNDDI
VEPLTERILG RVSVHDVFHI ISNELLVSSG QEITEEIARS IDDSGIESVE IRSVLTCESR
RGCCAKCYGR NLSSGQMVGI GESVGVIAAQ SIGEPGTQLT LRTFHVGGTA SNITVDANIK
AKFDGVVAFD DLRVIQSTNL EGDKVTVVMG RSGEIRIVEP VSGKTLLSNH VPYGAFLNVK
DGETVKKGQE LCFWDPYNAV ILSEFEGTIQ FDSIEEGVTY REESDEQTGH REKVIVDTKD
KTKNPAIIVN HKKGEPKGYS IPVGAHLAVE DGQDVKPGQV LVKIPRSVGK TRDITGGLPR
VTELFEARNP SNPAVVSEID GIVTYGAIKR GNREIFIESK DGVKKRYMVP LSKHILVQDN
DFIRSGNPLT DGAITPSDIL SIKGPTAVQE YLVNEIQEVY RLQGVKINDK HIEIIVRQMM
QKVQIIEAGD TSFLTNQAVD RFKFREENDN ILDKKVVVEC GDSEKLRPGM IITARQLRDE
NSSLKRKDQR LVVVRDAEPA VSMPTLQGIT QASLDTESFI SAASFQETTK VLSEAAVRGK
VDFLKGLKEN VIVGHLIPAG TGQRVFNDII VGSKEEYDSL IASKEAFNAA RKGELQQS
