ID X5HM99_9RICK Unreviewed; 1375 AA.
AC X5HM99;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322,
GN ECO:0000313|EMBL:AHX11575.1};
GN ORFNames=NHE_0640 {ECO:0000313|EMBL:AHX11575.1};
OS Neorickettsia helminthoeca str. Oregon.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11575.1, ECO:0000313|Proteomes:UP000023755};
RN [1] {ECO:0000313|EMBL:AHX11575.1, ECO:0000313|Proteomes:UP000023755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon {ECO:0000313|EMBL:AHX11575.1,
RC ECO:0000313|Proteomes:UP000023755};
RA Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L., Fraser C.M.,
RA Dunning Hotopp J.C., Rikihisa Y.;
RT "Sequencing and Comparison of Genomes and Transcriptome Profiles of Human
RT Ehrlichiosis Agents.";
RL Submitted (MAR-2014) 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:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|HAMAP-Rule:MF_01322,
CC ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CP007481; AHX11575.1; -; Genomic_DNA.
DR RefSeq; WP_038559794.1; NZ_CP007481.1.
DR STRING; 1286528.NHE_0640; -.
DR KEGG; nhm:NHE_0640; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000023755; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 3.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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 NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01322};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000023755};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 236..515
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 881
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1375 AA; 152465 MW; 66474BCE9433E32A CRC64;
MKNFSSFHRS ADGSVDFDSI KISLASADKI RALSYGEVTK PETINYRTFK PERDGLFCAK
IFGPTKSYEC LCGKYKKIKY SGVVCERCGV EVTSSRVRRE RMGHIELASP VAHIWFLKSL
PSKICTLLDL TLKNVEKILY FESYVVIDPG VTAFNKNDII TDESYSEAIR EYGAGSFTAM
IGAEAIKHML ASLNLEEMAV KLRSQAASTN SEVKKKKIIK TLRLVEQFLG SDSRPVDMIL
DVIPVMPPDL RPLVMLDGGR FATSDLNALY RSVINRNNRL KSLIYLRAPS IIINNERRML
QEAVDALFDN GRRTKIIKGS NKRPYKSISD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ALELHQCGLP KKIALELFKP FIYSKLELYG IAPTIKTARR MVQNEQPEVW DVLAKVIHQH
PVFLNRAPTL HRLSVQAFEP VLIEGKAIQL HPLVCTAFNA DFDGDQMSVH VPLSIEAQVE
ARLLVMSTNN ILNPANSRPI IVPSKDIVLG VYYLSLEEKS QEVHPTVFCA PWEAEHAFVN
KKIALHTRIR CQLEFNGESR LYTTTFGRLQ LLKILPEGVP FDSVNTMLTV RDISNLVDLV
YKICGHGKTV EFADKIMELG FRYATLSGIS FGKDDMVVPA TKAEHVRKTN EEVKDYEFQY
QEGLITKHEK YNKVVDAWQK CTDIVAKDMM EGISVYENVA EMNSIFMMAQ SGARGSAAQI
KQLAGMRGLM AKPSGEIIPN PIISNLREGQ GVLEYFNSTH GARKGLADTA LKTANSGYLT
RRLVDVAQDS IIVEEDCGAT DGLMVRASIE GGVVIMPLSD SIFSRVSAGD IVDPSDGSTI
VRAGEMFDDA SIERIESLGI DSVRIRSVLT CKSKYGICRK CYGADLSNRK LVSLGEAVGV
IAAQSVGEPG TQLTMRTFHV GGAATRRVES SSMVAFCSGR VKFVNANLIT NRDGNYIVLS
RSFELLLVDS LGIEHFQGRV QYGGTVYVKE GDMVPIGKKL ADWDLYTVPI ISEASGKVSY
ADMIEGVSYN EIQDENTGIS NKTVVDWKQG EAASNLRPRV EILNADGSLA TGQQSKEAIY
LLPLGAILNV SPEDMVEAGD IIAKITKEST TTRDITGGLP RVIKLFEARK GKVNAVISEV
DGYVEFAKDY YKSKRKVLIR SREDSQRVYE YLVPKGRHLI VSEGDFIRKG EPLMDGDPDL
HEILRVLGLE ALAEYMITEI QRVYRLQGVK INNKHIEVII RKMLQKVEIT DAGDTTLLVG
EQVEKSRVEK INEVIATQGL RCASYTPVLL GITRASLQTE SFISAASFQE TTKILTEAAV
AGKVDRLRGL KENIIAGRLL PVGAGYFIDK LRHQFASEEQ HGQASVELGD DIASV
//
