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Entry: A0A095Z2F3_9BURK
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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
//
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