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Database: UniProt
Entry: A0A0A0DRT1_9BURK
LinkDB: A0A0A0DRT1_9BURK
Original site: A0A0A0DRT1_9BURK 
ID   A0A0A0DRT1_9BURK        Unreviewed;      1417 AA.
AC   A0A0A0DRT1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
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   ORFNames=JY96_12625 {ECO:0000313|EMBL:KGM40603.1};
OS   Aquabacterium sp. NJ1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Aquabacterium.
OX   NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM40603.1, ECO:0000313|Proteomes:UP000029993};
RN   [1] {ECO:0000313|EMBL:KGM40603.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM40603.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Masuda H.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGM40603.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM40603.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT   "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT   NJ1, capable of utilizing both liquid and solid n-alkanes.";
RL   Submitted (OCT-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}.
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:KGM40603.1}.
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DR   EMBL; JRKM01000001; KGM40603.1; -; Genomic_DNA.
DR   RefSeq; WP_035037900.1; NZ_JRKM01000001.1.
DR   STRING; 1538295.JY96_12625; -.
DR   eggNOG; COG0086; Bacteria.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000029993; 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   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01322};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000029993};
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          233..512
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1397..1417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         813
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         894
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"
SQ   SEQUENCE   1417 AA;  155718 MW;  1F31C786FF88EF20 CRC64;
     MKGLLDLFKQ FTPDEHFDAI KIGLASPEKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
     IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRD RMGHIELAAP CAHIWFLKSL
     PSRLGLVLDM TLRDIERVLY FEAYVVVDPG MTPLKKFSIM SEDDYDAKRI EYGDEFEALM
     GAEGIKKLLE EMDLDVEIDK LRNDMTGSEL KIKKNAKRLK VMEAFKKSGI KPNWMVMDVL
     PVLPPDLRPL VPLDGGRFAT SDLNDLYRRV INRNNRLARL LELKAPEIIV RNEKRMLQES
     VDSLLDNGRR GKAMTGANKR ALKSLADMIK GKSGRFRQNL LGKRVDYSGR SVITVGPTLK
     LHQCGLPKLM ALELFKPFIF ARLEAMGIAT TIKAAKKEVE SGTPVVWDIL EEVIKEHPVM
     LNRAPTLHRL GIQAFEPVLI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL SIEAQMEART
     LMLASNNVLF PANGEPSIVP SQDVVLGLYY ATRERINGKG EGMVFSDIPE LQRALDNGVV
     EITARINIRL TEYTKNKDTG EFVPETKLVE TTVGRALLSE ILPKGLPFAN INKALKKKEI
     SRLINTSFRK CGLKETVVLA DKLLQNGFRL ATRAGISIGI DDMLVPKEKY GLIERAEKEV
     KEIEQQYVSG LVTAGERYNK VVDIWGKTGD EVGKVMMSQL SKQKTIDRNG VEVDQESFNS
     IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ YFISTHGARK
     GLADTALKTA NSGYLTRRLV DVTQDLVVTE EDCGTDQGIA TRALVEGGEV IESLRDRILG
     RVPAIDVLHP ETQQVVITAG TMLDEDALDI LEAAGVDEVK VRTPLTCATR FGLCAKCYGR
     DLGRGGLVNS GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRAAIASSVE AKSDGIIGFN
     ATMRYVTNGK GDLVVISRSG EIIIADQHGR ERERHKVPYG AQLNVKADQT VKAGLILATW
     DPLTRPIITE FAGKAKFENV EEGVTVAKQV DEVTGLSTLV VIDPKRRGAA KVIRPQVKLL
     DASGAEVKIP GTDHAVTIGF QVGALIQVRD GQDLSPGEVL ARIPIEGQKT RDITGGLPRV
     AELFEARSPK DKGSLAEITG TVSFGKETKG KVRLQITDPE GKVWEDLVPK EKNILVHEGQ
     VVNKGESIVD GPADPQDILR LLGIEELARY IVDEVQDVYR LQGVKINDKH IQVIVRQMLR
     RVQITNAGDT NYIVGEQVER SELLDTNDRM RAEGKMIATH SDVLLGITKA SLSTDSFISA
     ASFQETTRVL TEAAIMGKRD ELRGLKENVI VGRLIPAGTG MAFHQARKAK EEMDDSERRA
     IAMQEAQERA ALELAALDGD DDGADAAAPA EGGAAAE
//
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