RPOC_CARRP
ID RPOC_CARRP Reviewed; 1292 AA.
AC Q05FH9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=CRP_161;
OS Carsonella ruddii (strain PV).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX NCBI_TaxID=387662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV;
RX PubMed=17038615; DOI=10.1126/science.1134196;
RA Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA Hattori M.;
RT "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL Science 314:267-267(2006).
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 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC organisms. {ECO:0000305};
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, ECO:0000305}.
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DR EMBL; AP009180; BAF35192.1; -; Genomic_DNA.
DR AlphaFoldDB; Q05FH9; -.
DR SMR; Q05FH9; -.
DR STRING; 387662.CRP_161; -.
DR PRIDE; Q05FH9; -.
DR EnsemblBacteria; BAF35192; BAF35192; CRP_161.
DR KEGG; crp:CRP_161; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000777; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1292
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308826"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 746
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1292 AA; 150183 MW; 180AD521D41179C8 CRC64;
MIKSIFKKVS IKMASSSKIL SWSFGEVTHS NFINFKNLKP EPNGLFCLKI FSDFELCCLK
KKCFCHNDKF LNLKKAHTGY KVGHIKLFYP AVHIWYIKSS HSNISNILNL SYKILEKIIN
FKLKVVIKSY DIKIKKFNLF IFDKKIKNII FTLSGAKALK KLLSDRELFI DCLILKIKIK
KCNSFSKLFS ILKHINKILI FYYSGNKPSW MVLKKIPVLP PRMRPLIALS EKKFASSDIN
ELYKIVLERN YKLKKMTTYL DPKQLLINER ISLQESIYAL FDNEKLINPI LTSSKRVLKS
FSSLIKGKYG RFRQNLLGKR VDFSGRTVIT VEPNLFLYEC KIPIYIALEL FKPILYYELK
KKKIITTISF IDDYYKKNKK QIILLLKNKV KSYFIMLNRA PTLHRMNFQS FKILLTEDKT
IKIHPLVCLC YNADFDGDQM AIHLPLTNNA KVESNYLLLS INNIISPSNG NAIIIPTQDI
IMGIYYFTFD FKNKSISLND INDIINFFEF NNYNFQINIK FNNKKKINTT LGRIIINYLF
FKNFDYFLNI VFKKKILTYL IKYLFDFNQL SKIIIILEKL KKIGFLISTY SGITISYFDL
IEVKNTFLIN KVVFKLKYNN NIFSIVELLN NFFVKIIIKK IQINKTGLKK TNNLFIMLDS
GSRGSMLQIK QLIAFRGFFS KSNGDIIKDP IFDNLKNGLN MKNYFISTFG ARKGLTDTSL
KTANSGYLTR KLIDVSHDLV IYKIDCKTKT GIKIFLNSYF TLVELYKNLY GRLLLFSVSL
KNKILLKENT LIDNKVLFLL IKKKINTIFV RSVLFCISNR GVCCFCYGID LSTNKIVLIG
VSVGIISAQS IGEPGTQLTM RTFHTGGVAS YFFYSDNLII SNSGFVKFKK CKCVINKFGE
VIIVSLYGEF MIFNKIILEK YKFYYGTKIK FRNGFLIKKN TKLINFNDNN FYIYSENIGY
VYFKKENNIV KNYCLEDNKF YYKTLKNFKI TIINKSIKKN YFIPKNFNIV VYCYDYIFPG
EIIAKLVSVT ILKSSIIGGL PRLSELFEAR IPKLKALLSE IDGVCKIKFS HLNYIITIIS
KFGFYKEYTL SCLRKLYINN GDYVKIGDIL SDGKPDLNEI INLISINYLL SYFVNEINSI
YFPQNIYVNC KHIELILKQM TKKVKIIFSG ESSCQQGDIL FLEDAINENF STLVNSRRLS
YYKRIVTGIT KTSLESLSFF SAASFQETNK ILVNSAIKNR TDYLLGLKEN VLVGRLIPAG
TGLIKYFKKK SKSSKNNLDF KNRKKKFYIN YF
