RPOC_ANAMM
ID RPOC_ANAMM Reviewed; 1415 AA.
AC Q5PBG3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=AM263;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000030; AAV86366.1; -; Genomic_DNA.
DR RefSeq; WP_010263106.1; NZ_AFMU01000046.1.
DR AlphaFoldDB; Q5PBG3; -.
DR SMR; Q5PBG3; -.
DR GeneID; 7398649; -.
DR KEGG; ama:AM263; -.
DR PATRIC; fig|320483.3.peg.222; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
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..1415
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225505"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 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 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 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 879
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 886
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"
SQ SEQUENCE 1415 AA; 156718 MW; 84928C421A5BA9EC CRC64;
MKMLDLYGYT SIAQSFDKIC ISIASPESIR AMSYGEIKDI STTNYRTFKV EKGGLFCPKI
FGPVNDDECL CGKYRKKRYR GIVCEKCGVE VTSSKVRRER MGHIELVSPV AHVWFLKSLP
SRIGALLDMP MKSIESILYS GDFVVIDPMT TPFSKGEVIS ESVYNQARDA YGDEGFIALT
GAEAIRELLV RLDLGAIRAG LRSELESTSS EMKRKKVVKR LRIIENFIAS GNRPEWMILT
VIPVLPPDLR PLVSLENGRP AVSDLNHHYR TIINRNNRLE KLLKLNPPAI MIRNEKRMLQ
EAVDGLFDSS RRSYVSSRAG SMGYKKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
GLKLHQCGLP KKMALELFKP FICSKLKMYG VAPTVKLANK MIQSEKPEVW DVLDEVIREH
PILLNRAPTL HRLGLQAFDP VLIEGKAIQL HPLVCSAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPSNGRPI IVPSKDIVLG IYYLTLQRAQ APDQEVMSFG ELSHVEYALH
EGIVHTSSKI KYRMQRCNSD GTIVSEVVET TPGRLILWQI FPQHKDLTFD LVNQVLTVKE
ITSIVDLVYR SCGQRETVEF SDKLMCLGFQ YASQSGISFG CKDMIIPDTK AAHVENASEK
IKEFSIQYQD GLITRSERYN KVVDEWSKCT DLIARDMMKA ISLSDEEGKL NSIYMMANSG
ARGSASQMKQ LAGMRGLMAK PSGEIIETPI ISNFREGLSV FEYFNSTHGA RKGLADTALK
TANSGYLTRR LVDVAQDCTV VEYDCKTKDG VVARAVIEGG AVVATLDSVV LGRVAAVDTY
NPVTEELLLS AGELIDEGKV EKIRVAGLDA VRVRSPLTCE SKKGICSLCY GRDLAVGDLV
SIGEAVGVIA AQSVGEPGTQ LTMRTFHVGG TAMRGVEVSN LIAVLDAEVK LVNSNVVTDK
YGNQIVMSRS CEVVLLDSVG NEKMRHSVPY GAKLYVSDGQ PVKMMDKMAE WDPYTIPIIT
EKTGTIKYVD LIYGVSINEV LDESTGISNR VVIDWKLHLQ GANLRPRLVL LDEDGNIATL
YNDLEASYFV PIGAVLNVQD GQKVHAGDVI TRIPRESIKT RDITGGLPRV IELFEARRPK
EHAIVSDVDG YVEFGKDYYR SKRRIFIRPV DKSLPAVEYL VPKGKHTIVN EGDFVHKGDL
LMDGDPDQHD ILRVLGAEAL ASYMISEIQQ VYRLQGVRID NKHIEVILRQ MLQKVEITDP
GDTMYLVGEH AGREEVMRLN RKLEEAGKKP VAYVPILQGI TKASLDTNSF ISAASFQETT
KVLTEAAFSG KEDPLYGLKE NVIVGRLIPA GTGFIMNKVK KLAMLDQSDY ATYYNSELRE
IMGDLGDELI AEGEAASPGR SGDGYLGNGG GVVDY
