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Database: UniProt
Entry: K2IXD2_9RHOB
LinkDB: K2IXD2_9RHOB
Original site: K2IXD2_9RHOB 
ID   K2IXD2_9RHOB            Unreviewed;      1412 AA.
AC   K2IXD2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=B30_20863 {ECO:0000313|EMBL:EKE67302.1};
OS   Celeribacter baekdonensis B30.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE67302.1, ECO:0000313|Proteomes:UP000006762};
RN   [1] {ECO:0000313|EMBL:EKE67302.1, ECO:0000313|Proteomes:UP000006762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B30 {ECO:0000313|EMBL:EKE67302.1,
RC   ECO:0000313|Proteomes:UP000006762};
RA   Wang W.;
RT   "Celeribacter baekdonensis B30 Genome Sequencing.";
RL   Submitted (SEP-2012) 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:EKE67302.1}.
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DR   EMBL; AMRK01000023; EKE67302.1; -; Genomic_DNA.
DR   RefSeq; WP_009574249.1; NZ_AMRK01000023.1.
DR   STRING; 1208323.B30_20863; -.
DR   PATRIC; fig|1208323.3.peg.4288; -.
DR   eggNOG; COG0086; Bacteria.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000006762; 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:UP000006762};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          238..517
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
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         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         811
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         892
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"
SQ   SEQUENCE   1412 AA;  156932 MW;  C0E2FA053DC07C6B CRC64;
     MNQEITANPF NPMAQPTTFD EIKVSLASPE RILSWSYGEI KKPETINYRT FKPERDGLFC
     ARIFGPIKDY ECLCGKYKRM KYRGVVCEKC GVEVTLQKVR RERMGHIELA APVAHIWFLK
     SLPSRIGLML DMTLRDLERV LYFENYVVIE PGLTDLTYGQ MMTEEEFMDA QDLYGMDAFE
     ADIGAEAIRK MLGNIDLEST ADQLREDLKE ATGELKPKKI IKRLKIVESF LESGNRPEWM
     ILTVIPVIPP ELRPLVPLDG GRFATSDLND LYRRVINRNN RLKRLIELRA PDIIVRNEKR
     MLQESVDALF DNGRRGRVIT GANKRPLKSL SDMLKGKQGR FRQNLLGKRV DFSGRSVIVT
     GPELKLHQCG LPKKMALELF KPFIYSRLEA KGLSSTVKQA KKLVEKERPE VWDILDEVIR
     EHPVFLNRAP TLHRLGIQAF EPTLIEGKAI QLHPLVCSAF NADFDGDQMA VHVPLSLEAQ
     LEARVLMMST NNVLSPANGA PIIVPSQDMI LGIYYISMER EGMQGEGMVF SNIDEVEYAL
     SSGAVHLHAK VTARIKQIDE HGQEVWKRFE TTPGRLRLGG LLPLNAKAPF DLVNRLLRKK
     EVQQVIDTVY RYCGQKESVI FCDQIMSLGF KEAFKAGISF GKDDMVVPDN KWTLVDATRD
     QVRDFEQQYM DGLITQGEKY NKVVDAWSKC NDKVTEAMMS TISANKRDEN GAEMEPNSVY
     MMAHSGARGS VTQMKQLGGM RGLMAKPSGE IIETPIISNF KEGLTVLEYF NSTHGARKGL
     SDTALKTANS GYLTRRLVDV AQDCIVRQVD CGTELAITAE AAVNDGEVVA SLAERLLGRV
     AAEDVLRPGT DEVLVSKNEL IDERKADLIE AAGIASMRMR SPLTCEAEEG VCAMCYGRDL
     ARGTMVNQGE AVGIIAAQSI GEPGTQLTMR TFHIGGVAQG GQQSFQEANQ EGKALFRNAM
     LLENKHGEKI VMGRNMQLVI VDDQGVERAS YKLGYGTKVF AEEGKMIARG DKLFEWDPYT
     LPIIAEKGGK AKFVDLISGL SVRDDTDDAT GMTQKIVTDW RSVPKGGDLK PEILILGEDG
     EPVRNDVGNP VTYLMSVDAV LSIEDGQDIQ AGDVVARIPR EGAKTKDITG GLPRVAELFE
     ARRPKDHAII AEIDGYVRFG KDYKNKRRIS IEPSDETKEP VEYMVPKGKH IPVAEGDFVQ
     KGDYIMDGNP APHDILAIMG VEALAVYMID EVQEVYRLQG VKINDKHIEV IVRQMLQKWE
     ILDSGETTLL KGEAVDKAEF DEANAKAESK GGRPAKGQPI LLGITKASLQ TRSFISAASF
     QETTRVLTEA SVQGKRDKLV GLKENIIVGR LIPAGTGGAT KRVRRIAQER DNVVIEEARA
     EAEAAAQLAA PVMDVMGDEA ESLMVETPEG QE
//
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