ID A0A095Z2F3_9BURK Unreviewed; 1425 AA.
AC A0A095Z2F3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=HMPREF2130_09305 {ECO:0000313|EMBL:KGF28576.1};
OS Oligella urethralis DNF00040.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Oligella.
OX NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF28576.1, ECO:0000313|Proteomes:UP000029629};
RN [1] {ECO:0000313|EMBL:KGF28576.1, ECO:0000313|Proteomes:UP000029629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00040 {ECO:0000313|EMBL:KGF28576.1,
RC ECO:0000313|Proteomes:UP000029629};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_01322, 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:KGF28576.1}.
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DR EMBL; JRNI01000047; KGF28576.1; -; Genomic_DNA.
DR RefSeq; WP_036560269.1; NZ_JRNI01000047.1.
DR eggNOG; COG0086; Bacteria.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000029629; 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; 1.
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:UP000029629};
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 235..514
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
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 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 814
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"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1425 AA; 157473 MW; D9E9A1FD9C8106CA CRC64;
MNGLLSLYKQ IAPDEQFDAI KIGIASPEKI RSWSYGEVRK AETINYRTIK PERDGLFCAK
IFGPTKDYEC LCGKYKRLKH RGIICEKCGV EVTAAKVRRE RMGHIELASP VAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAMCVIEPG MTPLQRGQIM TEEEYNNKVD EYGDEFVALM
GAEAIRELLR TLDIDKEAET LREELKITTS EAKLKKISKR LKVVEGFQKS GIKPEWMILE
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLIESYAPDI IVRNEKRMLQ
EAVDSLMDNG RRGKAMTGQN KRQLKSLADM IKGKGGRFRQ NLLGKRVDYS GRSVIVVGPQ
LKLHQCGLPK LMALELFKPF IFHRLVAMDL VATTKAAKRL VEAQEPVVWD ILEEVIREHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSIEAQVES
RTLMLASNNI LFPASGEPSI VPSQDIVLGL YYTTRSRING KGEGSFFADL NELHRAYNTG
AVELQSRITV RLNEWVKDAN GEFQPQLKRV ETTVGRALLS EILPKGLPFS VIDKALTKKE
ISNLVSQAYR RCGLRETVIF ADKLMQSGFS LATKAGISIA VDDMLVPAAK VDILAQASEE
VKAIDKQHSS GLVTTQERYN NVVDIWGKAT ERVTKVMMEQ LATEKVMNRF DEEVDQESFN
SIYMMADSGA RGSATQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNVL QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVTQDLVII EDDCGTTNGY MIKAKVEGGE IIEPLRDRVL
GRVAAADIIN PDTQETVITA GTMLDEDAVE LIDKLGIDEV KIRTPLTCET RHGLCAQCYG
RDLGRGTLVN RGEAVGVIAA QSIGEPGTQL TMRTFHIGGA ASRTASVSSV ETKSNGKVAF
LASMRYVTNS KGERIAISNN GELLIVDPTT ERERERHRVP YGATVMVGDG DEVKAGAKLA
TWDPLTRPIV SEYAGQVKFD NIEEGVNVAQ QTDEVTGLST LVVITPKRAT RANVRPQIKM
LDEKGEELKI LGPNNTSHSV AISFPVGALI RVRDGQEIGV GEIVARIPVD SQKTRDITGG
LPRVVELFEA RSPKDAGILA DVSGVVSFGK DTKGKQRLVI TDTDGQPHEF LIPKEKHIQV
QNGRVVHQGE LIVDGPADPH DILRLKGIEM LAQYIIDEVQ EVYRLQGVKI NDKHIEVIVR
QMLRRVVVED AGDTSFIPGE QVERSALLDE NDRVQAEGGQ PATYQNILLG ITKASLSTDS
FISAASFQET TRVLTEAAVM GKRDELRGLK ENVIVGRLIP AGTGLAYHLA RHQKLDSRSS
FEHSSSTEQE NPFIEPVSLE SALGATAEAV TTELDSSKES GPTEE
//