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Database: UniProt
Entry: C6SJ09_NEIME
LinkDB: C6SJ09_NEIME
Original site: C6SJ09_NEIME 
ID   C6SJ09_NEIME            Unreviewed;      1391 AA.
AC   C6SJ09;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   13-SEP-2023, entry version 55.
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:CBA06644.1};
GN   ORFNames=NMW_0929 {ECO:0000313|EMBL:CBA06644.1};
OS   Neisseria meningitidis alpha275.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=295996 {ECO:0000313|EMBL:CBA06644.1};
RN   [1] {ECO:0000313|EMBL:CBA06644.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Alpha275 {ECO:0000313|EMBL:CBA06644.1};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, 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; AM889138; CBA06644.1; -; Genomic_DNA.
DR   SMR; C6SJ09; -.
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; 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   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; 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   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};
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          237..516
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
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         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         816
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1391 AA;  153734 MW;  048AA35223E495C8 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 RDGNEVDQES
     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 SRHQQWQGVE
     QETAETQVTD E
//
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