RPOC_PSYWF
ID RPOC_PSYWF Reviewed; 1406 AA.
AC A5WH34;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-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};
GN OrderedLocusNames=PsycPRwf_2035;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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; CP000713; ABQ94975.1; -; Genomic_DNA.
DR RefSeq; WP_011961249.1; NC_009524.1.
DR AlphaFoldDB; A5WH34; -.
DR SMR; A5WH34; -.
DR STRING; 349106.PsycPRwf_2035; -.
DR PRIDE; A5WH34; -.
DR EnsemblBacteria; ABQ94975; ABQ94975; PsycPRwf_2035.
DR KEGG; prw:PsycPRwf_2035; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
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..1406
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000073244"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 466
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 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1406 AA; 155676 MW; 93FD089B17E1745C CRC64;
MKDLLDIMKS PADNGKREFD SIQITLAAPE TIKSWSHGEV KKPETINYRT FKPERDGLFC
AKIFGPVKDF ECLCGKYKRR KFQGVICEKC GVEVTTAKVR RDRMGHIDLA SPVAHIWFLK
SLPSRIGLLL DMTLRDIERV LYFESYVVTD PGMTSLEKYQ LLDDEDYYKA LEEFGDEFIA
KMGAEAVQDL LKDIDIDLEI DDLREAIPNT GSETKLKKMS KRLKLLEAFR DSNNKPEWMV
MSILPVLPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LKRLLELNAP DIIVRNEKRM
LQESVDALLD NGRRGRAITG SNKRPLKSLA DMIKGKQGRF RQNLLGKRVD YSGRSVIVVG
PTLRLHQCGL PKKMALELFK PFTYSKLLSH GMATTIKQAK KMVEREEPQV WDMLAMVIRE
HPVLLNRAPT LHRLGLQAFE PVLIEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLTLEAQL
EARTLMMSTN NILSPANGDP IIVPSQDVVL GLYYISRSAV NAKGEGMIFA TVNEALRAIG
SNDLHVNAKI KVRVTETIFD EEGNSTKQTT LQETVAGRLL IWNVMPKGMR FAECNVEMTK
KNISKLMNSC YRTRGVKESV IFADQLMYLG FAQATLSGVS IGIEDMVIPP MKKELIEAAD
AEVREIEQQF EQGFVTAGER YNKVVDIWSR TNDKVAKAMM DNLATDIVIN AQGEEEEQKS
FNSIFIMSDS GARGSAAQIR QLAGMRGLMA KPDGSIIETP IKANFREGLS VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVAQDLV ITENDCGTEK GVRMTPHIQG GEIIEKLGDR
VLGRVVARDV MSREDEVLLA AGTLIDEHGV TVIDDNGIDE VWVRSVITCD VPHGVCAQCY
GRDLARGHKV NIGESVGVMA AQSIGEPGTQ LTMRTFHVGG AASSTSVDNS ISARNTGFIR
FHNMKTVDHV DGHLVIVSRS AEIGIADDVG RERERYKVPY GSSVLVKDGD EVESGQAIAK
WDPHTHPIIT EFAGKARFSD IIDGSTATVK IDEATGMSSF EILGSKDRPS NSKDLRPAII
LDTTGGKEVV YFLPAETIIR VSDGEEVTAG SVLGRVPQAT SGTKDITGGL PRVADLFEAR
RPKDHAIMAE MSGVVSFGSS TKGKNRFIIT NEDGEVHEEL IPKWRQINVF ENETVARGEV
IADGPLNPHD ILRLQGETAL ANYIVDEVQD VYRLQGVKIN DKHIEVIIRQ MLRKVEITDA
GDSNYFKGDQ VEYADVKATN EKLLAEDKFP VQFERQLLGI TKASLATESF ISAASFQETT
RVLTAAAVEG KVDELRGLKE NVVVGRLIPA GTGLAYHAAR KKAKEGKPAY DVESALDAAF
DIEATTSAQD FRSFDEAFAQ ELSQDK
