ID A0A3R8QR77_9FLAO Unreviewed; 1438 AA.
AC A0A3R8QR77;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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 ECO:0000313|EMBL:RRO17809.1};
GN ORFNames=EIG84_06655 {ECO:0000313|EMBL:RRO17809.1};
OS Flavobacteriaceae bacterium 14752.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2491711 {ECO:0000313|EMBL:RRO17809.1, ECO:0000313|Proteomes:UP000274596};
RN [1] {ECO:0000313|EMBL:RRO17809.1, ECO:0000313|Proteomes:UP000274596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14752 {ECO:0000313|EMBL:RRO17809.1,
RC ECO:0000313|Proteomes:UP000274596};
RA Yu Y.;
RT "Wangjiella luteus gen. nov., sp. nov., a novel bacterium of the family
RT Flavobacteriaceae isolated from a saline lake.";
RL Submitted (NOV-2018) 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}.
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:RRO17809.1}.
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DR EMBL; RRZV01000058; RRO17809.1; -; Genomic_DNA.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000274596; 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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 252..531
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 899
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"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1438 AA; 161176 MW; D10F66F91556B302 CRC64;
MTRHNDKNTQ VKFNQISIGL ASPEKILGES RGEVLKPETI NYRTHKPERD GLFCERIFGP
VKDYECACGK YKRIRYKGIV CDRCGVEVTE KKVRRDRVGH INLVVPVAHI WYFRSLPNKL
GYLLGIPSKK LDMIIYYERY VVIQAGEAKN EDGEPLQKMD FLTEEEYLNI LDSLPQENQY
LEDDDPNKFI AKMGAECLIE ILKRIDLDEL SYDLRHKANH ETSKQRKTEA LKRLQVVEAL
RDSKNNRNNN PEWMIMKVIP VIPPELRPLV PLDGGRFATS DLNDLYRRVI IRNNRLKRLM
EIKAPEVILR NEKRMLQESV DSLFDNTRKS SAVKTDSNRP LKSLSDSLKG KQGRFRQNLL
GKRVDYSARS VIVVGPELKM YECGLPKDMA AELYKPFIIR KLIERGVVKT VKSAKKIIDK
KEPIVWDILE NVLKGHPVLL NRAPTLHRLG IQAFQPKLIE GKAIQLHPLA CTAFNADFDG
DQMAVHLPLG PEAILEAQLL MLASHNILNP ANGSPITVPS QDMVLGLYYM TKERKSDKDY
KMKGEGLTFY SFEEVNIALN ERKVELNTSI KVRIKDNDPK AEKPYKIIES TVGRVIFNEH
LPEQVDYVND VLTKKALRKV ISDVIKKTSI PETAEFLDKI KSLGYNYAFK GGLSFSLGDI
IIPEEKQQLI DEANAQVETI VGNYNMGLIT NNERYNQVID IWTATNANLT ELAMKRITED
KQGFNSVYMM LDSGARGSKE QIRQLTGMRG LMAKPKKSTS GGGEIIENPI LSNFKEGLSI
LEYFISTHGA RKGLADTALK TADAGYLTRR LVDVSQDVIV REEDCGTLRG IEVSALKKND
EVVETLGERI VGRTSLNEVK DPISGEHILE AGEEITEEKA EMVENSALNS LEVRSPLSCE
SKKGICVKCY GRNLSTGKTV QRGEAVGVIA AQSIGEPGTQ LTLRTFHVGG IAGNISEDNK
LEANFDGKAE IEDLKTVNSK DNEGNDIKVV ISRTSELKLV DKKSGVVLST NVIPYGSQLF
IKPGAMVKKG DVICKWDPYN GVIISEFSGQ VKFENIEQGL TYKIETDEQT GFQEKVISES
KNKRKIPTLH ILNTKGENIR SYNLPVGAHL IVDDEEKIDE GKILVKIPRS SSKAGDITGG
LPRLTELFEA RNPSNPAVVS EIDGVVSFGK IKRGNREIII ESKLGETKKY LVKLSNQILV
QENDYVRAGM PLSDGSVTPN DILNIKGPSA VQQYLVNEVQ EVYRLQGVQI NDKHFEVVVR
QMMQKVKIKD SGDTTFLENQ LVHKQDFIEE NDNIFAKKVV EDPGDSQNLK AGQIVTLREL
RDENSILKRE DKKVVEARDA ESATAIPVLQ GITRASLQTK SFISAASFQE TTKVLNEAAV
SGKIDKLEGL KENVIVGHKI PAGTGLREFD DIIVGSEEEL DNMLKPEDMQ PNVSVNLN
//
