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RPOC_NEIMB
ID   RPOC_NEIMB              Reviewed;        1391 AA.
AC   Q9K1J1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=NMB0133;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40592.1; -; Genomic_DNA.
DR   PIR; F81233; F81233.
DR   RefSeq; NP_273191.1; NC_003112.2.
DR   RefSeq; WP_002218564.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1J1; -.
DR   SMR; Q9K1J1; -.
DR   STRING; 122586.NMB0133; -.
DR   PaxDb; Q9K1J1; -.
DR   EnsemblBacteria; AAF40592; AAF40592; NMB0133.
DR   KEGG; nme:NMB0133; -.
DR   PATRIC; fig|122586.8.peg.173; -.
DR   HOGENOM; CLU_000524_3_1_4; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000000425; 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..1391
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067768"
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;  153762 MW;  18FCEAE6CAC5D50E 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 EKAALLAEAN
     AEVKEIEDQY RQGLVTNGER YNKVVDIWGR AGDKIAKAMM DNLSKQKVID RAGNEVDQES
     FNSIYMMADS GARGSAAQIK QLSGMRGLMA KPDGSIIETP ITSNFREGLT VLQYFIATHG
     ARKGLADTAL KTANSGYLTR RLVDVTQDLV VVEDDCGTSD GFVMKAVVQG GDVIEALRDR
     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 VTDVDGVAYE TLISKEKQIL
     VHDGQVVNRG ETIVDGAVDP HDILRLQGIE ALARYIVQEV QEVYRLQGVK ISDKHIEVII
     RQMLRRVNIA DAGETGFITG EQVERGDVMA ANEKALEEGK EPARYENVLL GITKASLSTD
     SFISAASFQE TTRVLTEAAI MGKQDELRGL KENVIVGRLI PAGTGLTYHR SRHQQWQEVE
     QETAETQVTD E
 
 
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