ID   A0A1G3Z2H6_9BACT        Unreviewed;      1386 AA.
AC   A0A1G3Z2H6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   11-DEC-2019, entry version 15.
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=A2007_00700 {ECO:0000313|EMBL:OHE71096.1};
OS   Verrucomicrobia bacterium GWC2_42_7.
OC   Bacteria; Verrucomicrobia; unclassified Verrucomicrobia.
OX   NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE71096.1, ECO:0000313|Proteomes:UP000184561};
RN   [1] {ECO:0000313|EMBL:OHE71096.1, ECO:0000313|Proteomes:UP000184561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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       ECO:0000256|SAAS:SAAS00054030}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-Rule:MF_01322,
CC         ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS01121830};
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|SAAS:SAAS01207260};
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01322}.
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:OHE71096.1}.
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DR   EMBL; MIDO01000115; OHE71096.1; -; Genomic_DNA.
DR   Proteomes; UP000184561; Unassembled WGS sequence.
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; -; 2.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime.
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; IPR038120; Rpb1_funnel_sf.
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 {ECO:0000256|HAMAP-Rule:MF_01322,
KW   ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442970,
KW   ECO:0000313|EMBL:OHE71096.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|SAAS:SAAS01207259};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01322,
KW   ECO:0000256|SAAS:SAAS01207262};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01322,
KW   ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442967};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01322,
KW   ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442998};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01322,
KW   ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00443006};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|SAAS:SAAS01207265}.
FT   DOMAIN          237..516
FT                   /note="RPOLA_N"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1365..1386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1368..1386
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           71
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           73
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           86
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           89
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           462
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           464
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   METAL           466
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1386 AA;  152998 MW;  6F73DD8413538F50 CRC64;
     MSTQEVRDIL GFDQEQVFDY VGIAIAAPDV MRSWSKGEVK NPETINYRTF KPEPGGLFCQ
     RIFGPVRDYE CACGKYKRIK YKGVVCDRCG VEVTVSRVRR DRMGHIELAV PISHIWFLKS
     MPSRVGLLLD MTARDLEKVI YYENYIVIDP GKTPLEKKAL LSEQEFLQLQ EEYGDDAFFA
     KMGAEAIRIL LAELDLAQMV QEIEEEIHSS RSKQSKKKLA KRLKIISGFL NSGTRPEWMV
     LEVLPVIPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LKNLLQLKTP DVIINNEKRM
     LQESVDALFD NGRHGRPVTA AGNRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVIG
     PELRLHQCGL PKKMALVLFE PFIIRRLKEL GFVHTVRGAR KMIENKSPEV WDILEEVTKG
     HPVLLNRAPT LHRLSIQAFE PQLIEGDAIR LHPLVCSAYN ADFDGDQMAV HVPLSLEAIL
     ESKLLMLASN NIFSPSSGKP VLTPSQDIVL GSYYLTVEPR RKPSEGERVP LLQSTREALA
     AEVEGMLSKH QWVDFVNPDF GRKTIFGNAA KKIIRTTVGR VIYNSIWPKS LGFVNGPVAK
     SKLGDMILNL YKIASTKQEA VDTLDRLKEM GFKIATKAGI SIGIGDMIIP TEKSGIVNKS
     RKRLEEVDSQ YQKGIITEGE RTNKVIDIWS SATDEIAKAT FACLESNEGK EGINPVFLMM
     DSGARGNRQQ VRQLCGARGL MAKPSGEIIE RPILSSFREG LSVLEYFVST HGTRKGLADT
     ALKTADAGYM TRKLCDVAMD CIISSLDDGN RDGVWKHAIY EGDDEVVKLS DRIVGRCSSE
     DVYSPLNPDE ILVKSGEILT PEVAEKIEDL GIDRVKIMSP LTHLKRGGLS AKAYGIDPAT
     NKLVEMGTAV GIIAAQSIGE PGTQLTMRTF HVGGVASQVL KNPEIRVRHN GQIKFKGLRL
     VQTADGASIV LNKTGSVIIM DKEDHELESY HIVAGAVLMV ADGSEIHKGD VLAMWDPHNI
     PILSEKGGSV GFKDMIPGVT VKRELDESTG RIATVVIEHK EDLNPTVEVK ALAGNKEGLS
     TGKVIATYAI PVGAQVVVHE GDEISPGALL AKTPRSASKT QDITGGLPRV AELFEARRPK
     DAAEMAKIDG IVSMGSTVRG KRRLIVSDTE TGQQEDHLIS HGRQIIVHVG DFVTKGQSLT
     EGAADPHEIL EILGPYAVQE YLISEIQKVY RLQGVVINDK HIELIVARML RKVRVTDPGD
     SDFFWGEQID RTAFIESNER IVEAGGQPGE GEPILLGVTK ASLETDSFIS AASFQETTRV
     LTEASTLGKV DKLSGFKENV IMGQLIPAGT GFHKYRRLKV VPMGNESVEP TDRSSQGKSV
     ELATIE
//