RPOC_PHOV8
ID RPOC_PHOV8 Reviewed; 1428 AA.
AC A6KYK2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=BVU_0812;
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; CP000139; ABR38516.1; -; Genomic_DNA.
DR RefSeq; WP_005844836.1; NC_009614.1.
DR AlphaFoldDB; A6KYK2; -.
DR SMR; A6KYK2; -.
DR STRING; 435590.BVU_0812; -.
DR PRIDE; A6KYK2; -.
DR EnsemblBacteria; ABR38516; ABR38516; BVU_0812.
DR GeneID; 66751849; -.
DR KEGG; bvu:BVU_0812; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; BVUL435590:G1G59-854-MON; -.
DR Proteomes; UP000002861; Chromosome.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 4.10.860.120; -; 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 PANTHER; PTHR19376; PTHR19376; 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 TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1428
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308820"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1428 AA; 158839 MW; 4D76547EE7BB8149 CRC64;
MAFRKETKIK SNFSKISIGL ASPEEILENS SGEVLKPETI NYRTYKPERD GLFCERIFGP
VKDYECHCGK YKRIRYKGIV CDRCGVEVTE KKVRRERMGH IQLVVPVAHI WYFRSLPNKI
GYLLGLPTKK LDAIVYYERY VVIQPGVKAE DGINKYDLLS EEEYLDILDT LPKENQYLED
TDPNKFIAKM GAEAIYDLLS TLDLDALSYE LRHKASNDSS QQRKNEALKR LQVVESFRAS
RGRNKPEWMI VRIVPVIPPE LRPLVPLDGG RFATSDLNDL YRRVIIRNNR LKRLIEIKAP
EVILRNEKRM LQEAVDSLFD NSRKSSAVKT DANRPLKSLS DSLKGKQGRF RQNLLGKRVD
YSARSVIVVG PELKMGECGI PKLMAAELYK PFIIRKLIER GIVKTVKSAK KIVDRKEPVI
WDILEHVMKG HPVLLNRAPT LHRLGIQAFQ PHMIEGKAIQ LHPLACTAFN ADFDGDQMAV
HLPLSNDAIL EAQMLMLQAH NILNPANGAP ITVPAQDMVL GLYYITKLRK GAKGEGLTFY
GPEEALIAYN EGKVDIHAIV NVVVKDLDKD GKIVDVMMKE TSVGRVIVNE IVPAEVGYLN
TIISKKSLRD IISDVIKAVG VARACEFLDG IKNLGYYMAF KGGLSFNLGD IIIPKEKEEL
VKRGNEEVEQ IMMNYNMGFI TDNERYNQVI DTWTHVNSDL SDILYKTIKN DDQGFNSVFM
MLDSGARGSK EQIRQLSGMR GLMAKPQKAG AEGAQIIENP ILSNFKEGLS VLEYFISTHG
ARKGLADTAL KTADAGYLTR RLVDVSHDVI INEEDCGTLR GLVCTALKNN DEVIATLYER
ILGRVSVHDI VHPTTGKLIV AGGEEITEDI AQEIEDSPIE SVEIRSVLTC ESKKGVCAKC
YGRNLASSRM VQKGEAVGVI AAQSIGEPGT QLTLRTFHAG GIAGNMAANA SIVAKNNARL
EFEELRTVDT VDEMGEAVKV VVGRLAEVRF IDVNTGIILS THNVPYGSKL YAADGDIVEK
GKLIAKWDPF NAVIITEATG KIEFESVVEN VTYKVESDEA TGLREIIIIE SKDKTKVPSA
HIVTEDGNLI RTYNLPVGGH VVVENGQAVK AGDIIVKIPR AVGKAGDITG GLPRVTELFE
ARNPSNPAVV SEIDGEITMG KIKRGNREII VTSKTGEVKK YLVNLSKQIL VQENDYVRAG
TPLSDGAITP ADILAIKGPT AVQEYIVNEV QDVYRLQGVK INDKHFEIIV RQMMRKVEID
EPGDTRFLEQ QVVDKQEFME ENDRIWGKKV VVDSGDSQNL QPGQIVTARK LRDENSMLKR
RDLKPVEVRD AIPATSTQIL QGITRAALGT SSFMSAASFQ ETTKVLNEAA INGKVDRLEG
MKENVICGHL IPAGTGQREF EKIIVGSKEE YDRILANRKN VLDYSEVE
