ID K2LMX8_9PROT Unreviewed; 1395 AA.
AC K2LMX8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=TH2_20231 {ECO:0000313|EMBL:EKF06292.1};
OS Thalassospira profundimaris WP0211.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1177928 {ECO:0000313|EMBL:EKF06292.1, ECO:0000313|Proteomes:UP000007365};
RN [1] {ECO:0000313|EMBL:EKF06292.1, ECO:0000313|Proteomes:UP000007365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP0211 {ECO:0000313|EMBL:EKF06292.1,
RC ECO:0000313|Proteomes:UP000007365};
RX PubMed=23209215; DOI=10.1128/JB.01903-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Thalassospira profundimaris Type Strain WP0211.";
RL J. Bacteriol. 194:6956-6956(2012).
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:EKF06292.1}.
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DR EMBL; AMRN01000017; EKF06292.1; -; Genomic_DNA.
DR RefSeq; WP_008892338.1; NZ_AMRN01000017.1.
DR PATRIC; fig|1177928.3.peg.4126; -.
DR eggNOG; COG0086; Bacteria.
DR Proteomes; UP000007365; 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; 2.
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|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};
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 236..515
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1373..1395
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 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 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1395 AA; 154954 MW; A07F5EBD85C926B8 CRC64;
MNELMKIFGQ PQGTQSFDQI RIQIASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
IFGPVKDYEC LCGKYKRMKY RGIICEKCGV EVTLAKVRRE RMGHIELAAP VAHIWFMKSL
PSRLGLLLDM TLKDLERILY FENYVVIEPG LTPLKMGELL SEDQYMTAQE EYGEDSFRAG
IGAEAIRDML AAIDLDEERE TAKIDLKETN SEAKRKKLVK RLKLIEAFQE SGARPEWMIL
EVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIVRNEKRML
QESVDALFDN GRRGRPITGA NKRPLKSMSD MLKGKQGRFR QNLLGKRVDY SGRSVITVGP
NLKLHQCGLP KKMALELFKP FVYAKLELYG MATTIKAAKR MVEKERAEVW DILEQVIREH
PVMLNRAPTL HRLGIQAFEP TLIEGKAIQL HPLVCTAFNA DFDGDQMAVH VPLSLEAQLE
ARTLMMSTNN ILSPASGKPI IVPSQDIVLG LYYISMERDG QPGEGMSFVN IAEIEQALDE
GVVNLHSKVN ARYHTVDENN EPITVRVATT PGRMLLSELL PRHPRIPFST INKLLTKKDV
SNVIDVVYRH CGQKETVIFA DRMMGLGFNW ACKAGISFGK DDMIIPDAKE KLVGETHEKV
KEYEQQYQDG LITRGEKYNK VVDAWAQCTD DVSEAMMKVI SATAEGDNVN SVYMMAHSGA
RGSAAQMRQL AAMRGLMAKP DGSIIETPII SNFKEGLTVQ EYFNSTHGAR KGLADTALKT
ANSGYLTRRL VDVAQDCIIT QHDCGTDRGL DIAAVVDSGE VIETLSDRIL GRFTADEIVN
PSTGEIIVPK NEMVEEDHLD LIEKAGVEMA RIRSVLTCDA ETGVCGHCYG RDLARGTTVN
IGEAVGVIAA QSIGEPGTQL TMRTFHIGGA AQRGAEVSGV EANFDATVKL KNRAVVENSS
GVNIVMARNL EILLIDKTGR ERAKYRVPYG AKLLTDEGAQ VTRGQKLAEW DPYTLPIITE
KEGYVNYVDL LENVTIREVY DEATGIASKT VIDWKSMPKA SDLKPRVTLR NENGEVINLD
NGLEARYFLS VDAILSVENG QKVAAGDVLA RIPREGSKTR DITGGLPRVA ELFEARKPKE
HAIISDIPGR VEFGKDYKNK RRVVVHPLED SGLTEPVEYL IPKGKHLAVQ EGDFVEQGDQ
LLDGSPVPHD ILRVMGVPAL ADYLVNEIQE VYRLQGVKIN DKHIEVIVRQ MLQKVEITKP
GDTTLLVGEI IDRVDFDAEN ERALKEGGEL AEGAPVLQGI TKASLQTHSF ISAASFQETT
RVLTEAAVSG KTDTLIGLKE NVIVGRLIPA GTGAVMNRFR ALAAERDKNV QIEAEEEIGD
NFGPQSDTAS LPAGE
//
