RPOC_PSECP
ID RPOC_PSECP Reviewed; 1299 AA.
AC B8HD15;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Achl_2696;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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: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; CP001341; ACL40661.1; -; Genomic_DNA.
DR RefSeq; WP_015937858.1; NC_011886.1.
DR AlphaFoldDB; B8HD15; -.
DR SMR; B8HD15; -.
DR STRING; 452863.Achl_2696; -.
DR PRIDE; B8HD15; -.
DR EnsemblBacteria; ACL40661; ACL40661; Achl_2696.
DR KEGG; ach:Achl_2696; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002505; 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; -; 1.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1299
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165834"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 961
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1299 AA; 143390 MW; 1CF0E14653F49AB9 CRC64;
MSSESSFGLM QIGLATAEDI RGWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPSRDWEC
YCGKYKRVRF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLEKVIY FAAYMITSVD EAARHEELPN LQVEHDIEKK QLIDNRDGDI AAIARDLEGE
IARLEGEGAK AADKKKARDS ADRQMANVRK RADADIERLE QVWDRFKNLK VADLEGDEGL
YRELRDRYGM YFEGSMGAEA IKKRLEGFDM QAESDLLRDI IANGKGQRKT RALKRLKVVN
AFLTTNNSPL GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLLDL
GAPEIIVNNE KRMLQEAVDS LFDNGRRGRP VTGPGNRPLK SLSDMLKGKQ GRFRQNLLGK
RVDYSGRSVI VVGPQLKLHQ CGLPKQMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERYR
PQVWDVLEEI ITEHPVLLNR APTLHRLGIQ AFEPQLVEGK AIQLHPLVCG AFNADFDGDQ
MAVHLPLSPE AQAEARILML SSNNILKPSD GRPVTLPSQD MIIGLYHLTT KRKGSAGEGR
IFGSVSEAIM AFDARDLHLN SQVKIRLEGF VPYSGWEAPE GWEQGQPAIV ETSLGQVLFN
ETLPADYPWV EAVADKGELS RIVNDLAERY PKVVTAATLD NLKDAGFYWA TRSGVTVAIS
DIEVPAAKPE ILAGYEERAA KIQGQYDKGL IDDDERRQEL IEIWNKATND IAAVMRESLS
PMNTINRMVS SGARGNWMQV RQIAGIRGLV ANPKGEIIPR PIKSSYREGL SVLEYFIATH
GARKGLADTA LRTANSGYLT RRLVDVSQDV IVREEDCGTE RGLVTPIAVA DSNGELVLDE
NVENSAYART LAVDVVDSEG NVLAAAGTDC GDVVIDELFK AGITEVKVRS VLTCESSVGT
CALCYGRSLA TGKTVDIGEA VGIIAAQSIG EPGTQLTMRT FHTGGAVSAG GGDDITQGLP
RIQELFEART PKGVAPIAEA AGRITIEESE RQMRLVITPD DGTEEIAYPV LRRSRLLIED
GDHVTVGQKL INGPVDPKQV LRIMGPRAAQ KFLVDEVQGV YRSQGIGIHD KHVEVIVRQM
LRRVTVIESG ESDLLPGELA ERSRFEDANR RVVSEGKAPA SGRPELMGIT KASLATESWL
SAASFQETTR VLTQAAMEGK SDPLLGLKEN VIIGKLIPAG TGLPRYTEVT VEPTEEAKAN
LFTGPSAFSD FSYDTLGGDG APEFHAIPLD DYDLGNDFR
