RPOC_NEIMF
ID RPOC_NEIMF Reviewed; 1391 AA.
AC A1KRG7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=NMC0124;
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(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; AM421808; CAM09443.1; -; Genomic_DNA.
DR RefSeq; WP_002220157.1; NC_008767.1.
DR AlphaFoldDB; A1KRG7; -.
DR SMR; A1KRG7; -.
DR PRIDE; A1KRG7; -.
DR EnsemblBacteria; CAM09443; CAM09443; NMC0124.
DR KEGG; nmc:NMC0124; -.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002286; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1391
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308866"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
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 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1391 AA; 153862 MW; 86D445DF49716719 CRC64;
MNLLNLFNPL QTAGMEEEFD AIKIGIASPE TIRSWSYGEV KKPETINYRT FKPERDGLFC
AKIFGPVKDY ECLCGKYKRL KFKGVTCEKC GVEVTLSKVR RERMGHIELA APVAHIWFLK
SLPSRLGMVL DMTLRDIERV LYFEAFVVTD PGMTPLQRRQ LLTEDDYYNK LDEYGDDFDA
KMGAEGIREL LRTLNVAGEI EILRQELEST GSDTKIKKIA KRLKVLEAFH RSGMKLEWMI
MDVLPVLPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLLELHAP DIIVRNEKRM
LQEAVDSLLD NGRRGKAMTG ANKRPLKSLA DMIKGKGGRF RQNLLGKRVD YSGRSVITVG
PYLRLHQCGL PKKMALELFK PFIFHKLEKQ GLASTVKAAK KLVEQEVPEV WDILEEVIRE
HPIMLNRAPT LHRLGIQAFE PILIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQM
EARTLMLASN NVLSPANGEP IIVPSQDIVL GLYYMTRDRI NAKGEGSLFA DVKEVHRAYH
TKQVELGTKI TVRLREWVKN EAGEFEPVVN RYETTVGRAL LSEILPKGLP FEYVNKALKK
KEISKLINAS FRLCGLRDTV IFADHLMYTG FGFAAKGGIS IAVDDMEIPK EKVALLAEAN
AEVKEIEDQY RQGLVTNGER YNKVVDIWGR AGDKIAKAMM DNLSKQKVID RDGNEVDQES
FNSIYMMADS GARGSAAQIK QLSGMRGLMA KPDGSIIETP ITSNFREGLT VLQYFIATHG
ARKGLADTAL KTANSGYLTR RLVDVTQDLV VVEDDCGTSD GFVMKAVVQG GDVIEALRER
ILGRVTASDV VDPSSGETLV EAGTLLTEKL VDMIDQSGVD EVKVRTPITC KTRHGLCAHC
YGRDLARGKL VNAGEAVGVI AAQSIGEPGT QLTMRTFHIG GAASRAAAAS QVEAKSNGTA
RFSSQMRYVA NNKGELVVIG RSCEVVIHDD IGRERERHKV PYGAILLVQD GMAIKAGQTL
ATWDPHTRPM ITEHAGMVKF ENVEEGVTVA KQTDDVTGLS TLVVIDGKRR SSSASKLLRP
TVKLLDENGV EICIPGTSTP VSMAFPVGAV ITVREGQEIG KGDVLARIPQ ASSKTRDITG
GLPRVAELFE ARVPKDAGML AEITGTVSFG KETKGKQRLI ITDVDGVAYE TLISKEKQIL
VHDGQVVNRG ETIVDGAVDP HDILRLQGIE ALARYIVQEV QEVYRLQGVK ISDKHIEVII
RQMLRRVNIA DAGETGFITG EQVERGDVMA ANEKALEEGK EPARYENVLL GITKASLSTD
SFISAASFQE TTRVLTEAAI MGKQDELRGL KENVIVGRLI PAGTGLTYHR SRHQQWQEVE
QETAETQVTD E
