RPOC_BARHE
ID RPOC_BARHE Reviewed; 1402 AA.
AC Q6G3X4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BH06110;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27415.1; -; Genomic_DNA.
DR RefSeq; WP_011180535.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G3X4; -.
DR SMR; Q6G3X4; -.
DR STRING; 283166.BH06110; -.
DR PaxDb; Q6G3X4; -.
DR PRIDE; Q6G3X4; -.
DR EnsemblBacteria; CAF27415; CAF27415; BH06110.
DR GeneID; 64156890; -.
DR KEGG; bhe:BH06110; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000421; 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; 1.
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..1402
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225513"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
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 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1402 AA; 155586 MW; 1F325229D5F66BC1 CRC64;
MNHEVMNLFN PQSPAQTFDS IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRMK YKGIICEKCG VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
LPGRISTLLD LTLKDIERVL YFENYIVTEP GLTSLKLHQL LSEEEYMLAI DEFGEDQFTA
MIGAEAIYEL LASMELEKIA NDLRAELSET TSELKQKKLI KRLKIVENFL ESGNRPEWMI
MKTIPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP GIIVRNEKRM
VQEAVDALFD NGRRGRVITG ANKRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVTG
PELKLHQCGL PKKMALELFK PFIYARLDAK GYSSTVKQAK KLVEKEHPEV WDILDEVIRE
HPVLLNRAPT LHRLGIQAFE PVLIEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLSLEAQL
EARVLMMSTN NILHPANGAP IIVPSQDMVL GLYYLSIVSE KEPGEGMVFS DIGELHHALE
NKVVTLHTKI KGRVKNIDKD GKEVAKLYDT TPGRLIIGEL LPKNPSISFD IVNQEMTKKN
ISKMIDQVYR HCGQKETVIF CDRIMQLGFS HACRAGISFG KDDMLIPDSK LRLVAETEAL
AKEYEQQYND GLITQGEKYN KVVDAWGKCT DRVADEMMKR IQAVEFDPKT GRQRPMNSIY
MMSHSGARGS ANQMKQLAGM RGLMAKPSGE IIETPIISNF KEGLTVNEYF NSTHGARKGL
ADTALKTANS GYLTRRLVDV AQDAIISAVD CGTAKGLTMQ PIVDAGQIVA SLGQRILGRT
ALVDILHPVS GEVILEGGAM IEEADVAKIE EAGIQSVQIR SALTCETRLG VCAKCYGRDL
ARGTPVNQGE AVGVIAAQSI GEPGTQLTMR TFHLGGTAQV VDSSHLEASY EGTVEIRNRN
VVRNSEGHLV VMGRNMAILI KDGSGKERVV HRISYGAHIF VDDGDVVKCG QRIAEWDPYT
RPILTEVEGY VGFEDMIDGL SVTETADEST GITKRLVIDW RANPRGADLK PAIIIHADKK
GEAIAKYKGA EARYMMSVET ILSVEPGSHV KAGDVIARLP MESAKTKDIT GGLPRVAELF
EARRPKDHAI IAEVSGTIRF GRGYKNKRRI IIEPNDETLE PVEYLIPKGK LFHFQEGDQI
EKGDYILDGN PAPHDILAIK GVEALASYLV NEIQEVYRLQ GVLINDKHIE VIVRQMLQKV
EITESGDSGY IPGDHVDRIE LDEINDNLLA EGKRPASGNP ILLGITKASL QTPSFISAAS
FQETTRVLTE AAVSGKIDTL QGLKENVIVG RLIPAGTGGT IAQIRRIAAV RDDLIVDEQR
KSGNNEVAKA MLTNMTTVTT VE
