RPOC_HERA2
ID RPOC_HERA2 Reviewed; 1543 AA.
AC A9B6J1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Haur_0242;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000875; ABX02894.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B6J1; -.
DR SMR; A9B6J1; -.
DR STRING; 316274.Haur_0242; -.
DR PRIDE; A9B6J1; -.
DR EnsemblBacteria; ABX02894; ABX02894; Haur_0242.
DR KEGG; hau:Haur_0242; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000787; 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; 1.
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..1543
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141772"
FT REGION 1466..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 627
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1543 AA; 172905 MW; 380414A46E84E470 CRC64;
MLEINEFNAI RISLASPEDI LSWSHGEVTK PETINYRTLR PERDGLFCEK IFGPTRDWEC
YCGKYKRVRY KGIVCDKCGV EVTRSKVRRD RMGHIKLASP VSHIWFVKGT PSRLGLLLDI
SPRNLERVLY FASYIITDVD DLALGNVREQ MKTDFGVRRK DLEEKIIEQR GEKATRLSKD
LAAMDNAMEG TLERTHEQFA RQRQEIEDEA NALREHLEEL IGIDALADED IVYRGTVLLE
ENEPVRERSL EQLEQLIDQE REKLEQRREY EIENVRLLAD GERDQRQSVA DAEQERLTTA
LIKQLEDLNK EEKDKLDRLD DIQLHRIISE NEYRILRDLA PYTFKADMGA GAVRDIVSMV
DLDELSNQMQ AEVQSSSGQR RKKATKRLRV VEAFRKSGNR PEWMIMTVLP VIPPDLRPMV
QLDGGRFATS DLNDLYRRVI NRNNRLKRLM ELNAPEIIVR NEKRMLQEAV DALIDNGRRG
RPVSGKGKHR LKSLSDMLKG KQGRFRQNLL GKRVDYSGRS VIVVGPTLQL HQCGLPKKMA
LELFKPFVMR RLVDKGFAHN IKSAKRFVER VRPEVWDVLE EVIKDYLVLL NRAPSLHRLS
IQAFEAKLIE GSAIQLHPLV CAAFNADFDG DQMAVHVPLS RKAQEEARRR MISTYNLLSP
ATGDPIITPS QDIVLGCFYL TQVRPGAKGG GKRFGSIDEA LLAYTNGVVH IQAPVWIVIE
DYILPGSDLR EKELPSLDGV TPRVLIETSV GRIIFNNALR YQGEPKAGEN GYRSPLHYRN
FLVGKSGLKA LIADCYRFHS QRENIIADVY QELIERFGPE TSEESLLRFY ASERTARLAD
RIKALGFKHA TLGGMTFSAS DVEVPDTKDA IVQETYKKVQ DIEKMQRRGL ITDDERYREV
VTAWLDATNQ IKVEVQRSLN PFGPVSMMST SGARGNVEQI RQMAGMRGLT TDPTGRIIEL
PITANFREGL SVIEYFISTH GGRKGLADTA LRTADAGYLT RRLVDVAQDV IVTIEDCGTT
EGMWIRVSRD ILASVEDRIV GRVTVAPVTN PVTGEVIFDT DSEILEDDGK HIANVLKSLD
KEAQAEFGIY VRSVLTCNAD YGICRKCYGR NLATGKMVEI GEAVGIIAAQ SIGEPGTQLT
LRTFHTGGVA TDTDITQGLP RVQEIFEARI PKGKAVLAQI AGRVQIVREE EGIRRLRIVS
EEVYTDEQML PKDYRVVVKN GDAVEIGNLL AESNVDGDGR APLVAGLAGN VYVDDDRLVI
QAKDIEEHEE VIAHAARLRV KDGDLVQVGQ QMTEGSSDPQ EMLQLRGREA VQEYLTNEAQ
KVYRSQGVGI NDKHIEVIVR QMLRRVRIEE PGDTELLPGE LVELHELNRI NASIVSQGGD
PALAVPVLLG ITKASLSTDS FLSAASFQET TRVLTEAAVN GKIDYLRGLK ENVVIGKLIP
AGTGMEQRRK LAEEAALRVA QITSTPADRE VPAATPAPAV MSEPKPAPPR SFDEALNAVT
NIDSGNGPKD DLFAQAMARL QAEEGRKPTL SELLGTDEDE ENV
