ID E6L058_9PAST Unreviewed; 1422 AA.
AC E6L058;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:EFU66861.1};
GN ORFNames=HMPREF9064_1790 {ECO:0000313|EMBL:EFU66861.1};
OS Aggregatibacter segnis ATCC 33393.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU66861.1, ECO:0000313|Proteomes:UP000032871};
RN [1] {ECO:0000313|EMBL:EFU66861.1, ECO:0000313|Proteomes:UP000032871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU66861.1,
RC ECO:0000313|Proteomes:UP000032871};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU66861.1}.
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DR EMBL; AEPS01000014; EFU66861.1; -; Genomic_DNA.
DR RefSeq; WP_006719668.1; NZ_LS483443.1.
DR STRING; 739.GCA_001059425_01107; -.
DR GeneID; 60799231; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000032871; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000032871};
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 236..515
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 192..219
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 89
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 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1422 AA; 157979 MW; CD209FFE6B9A776A CRC64;
MKDLVKFLKA QSKTAEDFDV IKIGLASPDM IRSWSYGEVK KPETINYRTF KPERDGLFCA
RIFGPVKDYE CLCGKYKRLK HRGVICEKCG VEVTQTKVRR ERMGHIELAS PVAHIWFLKS
LPSRIGLLLD MPLRDIERVL YFESYIVIEP GMTDLERGQL LTEEQYLDAE DRWQDEFDAK
MGAEAIQALL RGIDLEAECE NLREELQETN SETKRKKITK RLKLLEAFLQ SGNKPEWMVM
TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLIAPD IIVRNEKRML
QESVDALLDN GRRGRAITGS NRRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP
YLRLHQCGLP KKMALELFRP FIYAKLESRG YATTIKAAKK MVEREDAIVW DILAEVIREH
PILLNRAPTL HRLGIQAFEP ILIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLTLEAQLE
ARALMMSTNN ILSPANGDPI IVPSQDVVLG LYYMTREKVN GKGEGMLLQD PREAEKAYRT
GQAELHSRVK VRITEYVKNE AGEFESKTTL TDTTIGRAIL WMIAPKGMPF SLFNQTLGKK
AISKLINESY RRLGLKASVM FADHIMYTGF AYAARSGSSV GIDDMVIPAK KYEIISAAEE
EVAEIQEQFQ SGLVTAGERY NKVIDIWAAA NERVAKAMME NLSTEEVINR EGKPEKQASF
NSIFMMADSG ARGSAAQIRQ LAGMRGLMAR PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVAQDLVI VEDDCGTHEG IVMTPLIEGG DEKVPLREQV
LGRVAAEDIL KPGTEEVLIP RNTLLDEKLC DVLDANSVDS VKVRSVVTCN TDFGVCAKCY
GRDLARGHLI NQGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASAAAKESS VQVKNNGTLR
LANAKFVTNN EGKLVLTSRN TELTVVDTFG RTKEHYKVPY GAILNKGDQQ EVNAGETIAN
WDPHTMPVIS EVSGFVKFVD IVDGLTVTRQ TDELTGLSSI VVQDVGERAT AGKDLRPAIK
LVDDKGNDIF VPGTDVVAQY FLPSKAIVTL DDGAEVHIGD PLARIPQESV GTKDITGGLP
RVADLFEARK PKEPAILAEI SGIVSFGKET KGKRRLLITP AEGEVYEEMI PKWRQLNVFE
GEMVERGDLI SDGAETPHDI LRLRGVHAVT EYIVNEVQEV YRLQGVKIND KHIEVIVRQM
LRKAIVTKAY DSEFLEGEQV EVARVKIVNR KREAEGKPPV EFERELLGIT KASLATESFI
SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGFAYHQNRH KNPAVIADEE
VPVRLSAADE EEIASEFVMT SEDASASLTE MLNMVEDDEH AE
//
