RPOC_SPHAL
ID RPOC_SPHAL Reviewed; 1427 AA.
AC Q1GT24;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Sala_1485;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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}.
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DR EMBL; CP000356; ABF53198.1; -; Genomic_DNA.
DR RefSeq; WP_011541778.1; NC_008048.1.
DR AlphaFoldDB; Q1GT24; -.
DR SMR; Q1GT24; -.
DR STRING; 317655.Sala_1485; -.
DR PRIDE; Q1GT24; -.
DR EnsemblBacteria; ABF53198; ABF53198; Sala_1485.
DR KEGG; sal:Sala_1485; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006578; 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; -; 2.
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; 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; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1427
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353441"
FT REGION 1393..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1427
FT /note="Basic and acidic residues"
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:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1427 AA; 158095 MW; E148EBEE82FA97CE CRC64;
MNQLTNFMNP VAKPETFDMI KIGIASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKY KGIVCEKCGV EVTVTKVRRE RMGHIELAAP VAHIWFLKSL
PSRIGLLLDM QLKQLERVLY FEAYIVLEPG LTPLEKFQLL TEDELLDAQD EYGEDAFSAG
IGAEAIRTLL ENLDLEQERT DLMEELATTK SELKPKKIIK RLKVVESFIE SGNRPEWMIL
EVVPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLMELRAPD IIVRNEKRML
QEAVDALFDN GRRGRTITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVTGP
ELKLHQCGLP KKMALELFKP FIYARLDAKG LSMTLKQAKK WVEKERKEVW DILDEVIREH
PVLLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPANGKPI IVPSQDMVLG LYYLSLEREG EPGEGMLLAD MAEVHQALHI
GAVTLHSKII SRVPQTDEKG NEYLKRFETT PGRMLIGECL PKSHTVPFDV VNRLLTKKEI
GDVIDQVYRH TGQKETVLFA DAIMALGFRH AFKAGISFGK DDMIIPASKE QLVDETRSLV
KDFEQQYQDG LITQQEKYNK AIDAWSQCGD KVANAMMDEI RATPKLPDGR LAPINSIYMM
AHSGARGSQA QMKQLAGMRG LMAKPSGEII ETPIISNFKE GLTVLEYFNS THGARKGLAD
TALKTANSGY LTRRLVDVSQ DCVVIEEDCG TTRGMEMRAI IQGGSTIASL GERILGRTTL
EDVVDKDGNV IAPVGTLLDE ATTQRIEEAE VQSVKIRSPL VCEATLGVCG KCYGRDLARG
TPVNIGEAVG VIAAQSIGEP GTQLTMRTFH IGGAAQVNEQ SNVEAISDGT IEYRDMATIV
DQRGRRLALS RSGEIAIIDS EGRERASHKL PYGAQIMHKD GEKVKKGDRI AEWDPFTMPL
ITEKQGVVKY QDLIDGKTLT EQVDEATGIA QRVVIEYRAA GRSKKEDLQP RITLLDDASG
EAARYLLAVG TMISVEDGQT VQAGDVLARV SREASKTRDI TGGLPRVAEL FEARIPKDNS
VIAKISGRIE FVKDYKAKRK IAIVPEEGDP IEYLIPKSKV LEVQEGDMVK RGDALISGSP
NPHDILDVMG VEALAEYLVA EIQEVYRLQG VKINDKHIEV IVRQMLQKVE ITDGGDTTLL
PGEQLDYLEM MEYNAKLPKN GKPAEGRPVL LGITKASLQT RSFVSAASFQ ETTRVLTEAS
VQGKVDSLQG LKENVIVGRL IPAGTGAAMN RVRVTASSKD AALRAAMRVA NQEHLIAPRT
AAEEHAAELA QGPEAAIGDD PLGKVQGEDF TTDDVMVEER PEGASEE
