ID A0A2V3ZZ56_9BACT Unreviewed; 1420 AA.
AC A0A2V3ZZ56;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PXY01563.1};
GN ORFNames=DF185_08755 {ECO:0000313|EMBL:PXY01563.1};
OS Marinifilum breve.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae.
OX NCBI_TaxID=2184082 {ECO:0000313|EMBL:PXY01563.1, ECO:0000313|Proteomes:UP000248079};
RN [1] {ECO:0000313|EMBL:PXY01563.1, ECO:0000313|Proteomes:UP000248079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC075 {ECO:0000313|EMBL:PXY01563.1,
RC ECO:0000313|Proteomes:UP000248079};
RA Fu T.;
RT "Marinifilum breve JC075T sp. nov., a marine bacterium isolated from Yongle
RT Blue Hole in the South China Sea.";
RL Submitted (MAY-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:PXY01563.1}.
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DR EMBL; QFLI01000003; PXY01563.1; -; Genomic_DNA.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000248079; 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 247..526
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 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 889
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 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1420 AA; 158280 MW; DBF32A5C837AE4C4 CRC64;
MAFRRDKQVK SNFTKISISL ASPEEILERS SGEVLKPETI NYRTYKPERD GLFCERIFGP
VKDYECHCGK YKRIRYRGIV CDRCGVEVTE KKVRRERMGH IQLVVPVAHI WYFKSLPNKI
GYLLGLPTKK LDTIIYYERY VVINPGVKSA DGIKYLDFLT EEEYLDILDE LPMENQFLDD
DDPNKFIAQM GAEALYSLLG RLDLDSLSYD LRHKANTETS QQRKNEALKR LQVVEAFRES
QGVNNPEWMI VKVVPVIPPE LRPLVPLDGG RFATSDLNDL YRRVIIRNNR LKRLIEIKAP
EVILRNEKRM LQEAVDSLFD NSRKSNAVKT ENNRPLKSLS DSLKGKQGRF RQNLLGKRVD
YSARSVIVVG PDLQMHECGL PKDMAAELYK PFVIRKLIER GIVKTVKSAK KIVDRKDPVV
WDILENVLKG HPVLLNRAPT LHRLGIQAFQ PKLIEGKAIR LHPLACTGFN ADFDGDQMAV
HLPLGNEAVL EAQMLMLCSH NILNPANGAP VTVPSQDMVL GLYYITKPRK GSKGEGLTFY
SAEEAMIAFN EKAVDLHSVI KVKVKDLNEN DELVDTIVET TIGRIILNQF TPEGAGFINQ
LITKKALRDI IGYVFKKCGV DACAKFLDDI KDLGYRKAFE GGLSFNLSDV IVPAEKEELV
AEGYAQVEEV LTNYNMGFIT NNERYNQIID IWTHVNANLT QTLMNQLIAD NQGFNSVYMM
LDSGARGSRE QIRQLGGMRG LMAKPQKSGA TGGQIIENPI LSNFKEGLSV LEYFISTHGA
RKGLADTALK TADAGYLTRR LVDVAQDVII NERDCGTLRG LTATAIKNQE EVVASLSERI
LGRTTVHDVY HPISGELIVK SGVEITEEIA QTIENSPIER VEIRSVLTCE SKQGVCAKCY
GRNLATGKAV QKGEAVGVIA AQSIGEPGTQ LTLRTFHVGG TAGNVSAENS VESKYDGYAE
FEELRTVEHT PEEGDKHDVV IGRLAELRII DKNTNITLTT HTIPYGSKLY IKDGQDVKKG
DLICEWDPYN AMIVTEFSGK VTFDNLIEGV TYKEESDEAT GFAEKVVVES KDKTKNPSVK
ILNSSGEVLK SYNLPVGAHI SVNEGEMVVS GQSVVKIPRA LGKAGDITGG LPRVTELFEA
RNPSNPAVVS EIDGEVTFGK IKRGNREIVV TTKTGDVKKY LVPLSKQILV QENDYVRAGT
PLSEGATTPA DILSIKGPTK VQEYIVNEVQ DVYRMQGVKI NDKHFEIIVR QMMRKVVIDD
PGDTKFLEKQ IIDKMEFMRE NDEIFGKKVV VDAGDSDELK AGQIVTARKL RDINSILKRR
DMKLVEAREA IAATSTQILQ GITRAALQTK SFISAASFQE TTKVLNEAAI SGKMDKLEGL
KENVICGHLI PAGTGLREYK DVVVGAKEEY EKLLDNKSEF
//
