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RPOZ_ANAMF
ID   RPOZ_ANAMF              Reviewed;         128 AA.
AC   B9KI83;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366};
DE            Short=RNAP omega subunit {ECO:0000255|HAMAP-Rule:MF_00366};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00366};
DE   AltName: Full=RNA polymerase omega subunit {ECO:0000255|HAMAP-Rule:MF_00366};
DE   AltName: Full=Transcriptase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366};
GN   Name=rpoZ {ECO:0000255|HAMAP-Rule:MF_00366}; OrderedLocusNames=AMF_324;
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida;
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(2009).
CC   -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C-
CC       terminal regions of the beta' subunit thereby facilitating its
CC       interaction with the beta and alpha subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00366}.
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_00366};
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_00366}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC       {ECO:0000255|HAMAP-Rule:MF_00366}.
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DR   EMBL; CP001079; ACM49195.1; -; Genomic_DNA.
DR   RefSeq; WP_012658906.1; NC_012026.1.
DR   AlphaFoldDB; B9KI83; -.
DR   SMR; B9KI83; -.
DR   STRING; 320483.AMF_324; -.
DR   EnsemblBacteria; ACM49195; ACM49195; AMF_324.
DR   GeneID; 7398433; -.
DR   KEGG; amf:AMF_324; -.
DR   PATRIC; fig|320483.3.peg.384; -.
DR   eggNOG; COG1758; Bacteria.
DR   HOGENOM; CLU_125406_2_1_5; -.
DR   OMA; NRFRLVI; -.
DR   OrthoDB; 1864134at2; -.
DR   Proteomes; UP000007307; 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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.940.10; -; 1.
DR   HAMAP; MF_00366; RNApol_bact_RpoZ; 1.
DR   InterPro; IPR003716; DNA-dir_RNA_pol_omega.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   TIGRFAMs; TIGR00690; rpoZ; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..128
FT                   /note="DNA-directed RNA polymerase subunit omega"
FT                   /id="PRO_1000133714"
FT   REGION          87..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   128 AA;  13896 MW;  E5A79181FA8515D2 CRC64;
     MREGDSGYFS CYDGNRFRLV ILASQRAHEL SSGACTAVAR KGDKNTVVAL REIVGEQLDL
     AAVFKLAVNR CRKYLEEFTN AREVAAARSS QAAPKSAPGQ EIGKSFREKD PSAAAFLDQE
     QFFSGGGE
 
 
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