ID A0A162KWR7_9BACL Unreviewed; 1205 AA.
AC A0A162KWR7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=PNBC_09070 {ECO:0000313|EMBL:OAB75213.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB75213.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB75213.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB75213.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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|ARBA:ARBA00006460, ECO:0000256|HAMAP-Rule:MF_01322,
CC 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:OAB75213.1}.
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DR EMBL; LSFN01000011; OAB75213.1; -; Genomic_DNA.
DR RefSeq; WP_068657349.1; NZ_LSFN01000011.1.
DR AlphaFoldDB; A0A162KWR7; -.
DR STRING; 1763538.LPB68_14775; -.
DR KEGG; pcx:LPB68_14775; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000077134; 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; -; 1.
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:UP000077134};
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 224..503
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1205 AA; 135214 MW; FEC9200CC68216AD CRC64;
MLDVNNFEYM KIGLASPEKI RSWSRGEVKK PETINYRTLK PEKEGLFCEK IFGPTKDWEC
HCGKYKRVRY KGVVCDRCGV EVTRAKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLALDM
SPRSLEEIIY FASYVVTDPG ETPLEKKQLL SEKEYRSYRE KYGYGFHAGM GAEAVKRLLQ
DIDVEKELEF LREELRTAQG QRRNRAIKRL EVIEAFRNSG NKPEWMIMDV LPVIPPELRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPDII VQNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPYL KMYQCGLPKK
MALELFKPFV MKELVNKGLA HNIKSAKRKV ERVSPEVWDV LEEVIKEHPV LLNRAPTLHR
LGIQAFEPIL VEGHAIRLHP LVCTAYNADF DGDQMAVHVP LSAEAQAEAR ILMLASGNIL
NPKDGKPVVT PSQDMVLGTF YLTMDNKEEK GTGMILRNVN EAVSAYQRGA AGLHARVAIP
AKALGKTNFT EKQQNAMLLT TIGKIIFNEI YPSSFPYINE ATRENLINGT PERYFVYDKG
ADIREKIQEL PISGAVGKEY LGQIIARCFE TYHTTETSVI LDDIKQLGFT YSTRAGITVA
VSDVIVPEEK VGILKESDAK VSVVTNQYRR GLITNEERYD RVIDIWSKTK DELTEVLMKS
MDRYNNIMMM VDSKARGNKS QITQLGGMRG LMANPSGRII ELPIKSNFRE GLTVLEYFLS
THGARKGLAD TALRTADSGY LTRRLVDVAQ DVIVREEDCG TDKGFTVTKI QDGKEVIEDL
YDRIEGRYCF ETVRHPETGE IIVNRNDLID SDKASAIIDA GVEKLQIRSV LSCRARHGVC
KTCYGRNLAT GKHVEIGEAV GIIAAQSIGE PGTQLTMRTF HTGGVAGDDI TQGLPRIQEL
FEARNPKGQA TISEIDGVVK EIRETKDRRE IEIQGEAETK TYLVTYGSRL RVSEGQEIEA
GDELTDGSID PKEILRIKGI RGVQNYILQE VQRVYRNQGV EINDKHVEVM IKQMLRKIRI
VDAGETTLLP GAFSDIHEYE AANKVAILSG KEPAVAKPVL LGITKASLET DSFLSAASFQ
ETTRVLTDAA IKGKVDKLLG LKENVIIGKL IPAGTGMNRY RSVTYADPEL QNKVLEEVVE
AVTID
//
