ID A0A1T4ZZ50_9SPHI Unreviewed; 1429 AA.
AC A0A1T4ZZ50;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05661099_0125 {ECO:0000313|EMBL:SKB28071.1};
OS Daejeonella lutea.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB28071.1, ECO:0000313|Proteomes:UP000189981};
RN [1] {ECO:0000313|Proteomes:UP000189981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUYR01000001; SKB28071.1; -; Genomic_DNA.
DR STRING; 572036.SAMN05661099_0125; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000189981; 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|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:UP000189981};
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 249..528
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1429 AA; 159823 MW; 313D983B067DEDB3 CRC64;
MSYKKDNKIK SNFTSITISL ASPESILERS SGEVLKPETI NYRTYKPERD GLFCERIFGP
VKDYECHCGK YKRIRYKGIV CDRCGVEVTE KKVRRERMGH INLVVPVAHI WYFRSLPNKI
GYLLGLPTKK LDLIIYYERY VVIQAGLKEA DGIQKMDFLT EEEYLDILDT LPKENQYLDD
KDPEKFIAKM GAEALQDLLG RLDLDQQSYD LRHQAATETS QQRKTEALKR LQVVEAFRGA
NTRIENNPEW MIVKIVPVIP PELRPLVPLE GGRFATSDLN DLYRRVIIRN NRLKRLIEIK
APEVILRNEK RMLQESVDSL FDNSRKVNAV KTEGNRALKS LSDILKGKQG RFRQNLLGKR
VDYSARSVIV VGPNLKLHEC GLPKDMAAEL FKPFIIRKMI ERGVVKTVKS AKKIVDRKDP
IVWDILENVL KGHPVLLNRA PTLHRLGIQS FQPKLVEGKA IQLHPLVCTA FNADFDGDQM
AVHLPLGNAA ILEAQMLMLA SHNILNPANG TPITVPSQDM VLGLYYITKG RRTDETRVVV
GQDQTFYSPE EVIIAYNERK LDLHAFIKVK TNVKEKDGGQ IVNKLIETTV GRVLFNQRVP
AEVGYINELL TKKSLRDIIG EVVKTTGMAR AAQFLDDIKE LGFQMAFQGG LSFNLQDLNI
PAEKAQLIGQ ASKEVEEVMN NYNMGFITNN ERYNQIIDIW TRINNRLTAN VMNQLSSDNQ
GFNSVYMMLD SGARGSKEQI RQLCGMRGLM AKPQKSGSGG EIIENPILSN FKEGLSVLEY
FISTHGARKG LADTALKTAD AGYLTRRLHD VAQDMIVGET DCGTLRGIYT TALKDNEDIV
EPLYDRILGR TSLHDVYDPL TNDLLVTAGE DIEEDVAVKI ENSALEGIEI RSVLTCESKR
GVCALCYGRN LATGKRVQMG EAVGVIAAQS IGEPGTQLTL RTFHVGGTAS NIAAESQIVA
KFDGVIEFEN VRTVSHQTEE GPLEVVLGRS GEFRIVEPGT NKMIMANNIP YGAYLYVKDG
EKISKGDKIC SWDPYNAVII SEFEGKAEFE AIIEGVTFRE ESDEQTGHRE KVIIDTRDKT
KNPVIRVADK KGNGLKGYNI PVGAHIAVEE HEAVKMGQII AKIPRSTGKT RDITGGLPRV
TELFEARNPS NPAVVTEIDG VVTLGGVKRG NREMSIESKD GQIKKYLVPL SKHILVQDND
FVKAGMPLSD GSISPADILS IKGPAAVQEY LVNGIQEVYR LQGVKINDKH FETIVHQMMQ
KVMIEDAGDT RFLEKELVDR WDFQLENDEI YDKRVVTDPG ESTNLKAGQI ISVRKLRDEN
SVLKRKDMRL VETRDAIAAT SSQMLQGITR ASLGTKSFIS AASFQETTKV LNEAAISGKR
DNLLGLKENV IVGHLIPSGT GLRHYERIIV GSQEEYDKLL ASKQEEVEA
//
