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Database: UniProt
Entry: R5J2K3_9FIRM
LinkDB: R5J2K3_9FIRM
Original site: R5J2K3_9FIRM 
ID   R5J2K3_9FIRM            Unreviewed;        88 AA.
AC   R5J2K3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000256|ARBA:ARBA00013725, ECO:0000256|HAMAP-Rule:MF_00366};
DE            Short=RNAP omega subunit {ECO:0000256|HAMAP-Rule:MF_00366};
DE            EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00366};
DE   AltName: Full=RNA polymerase omega subunit {ECO:0000256|HAMAP-Rule:MF_00366};
DE   AltName: Full=Transcriptase subunit omega {ECO:0000256|ARBA:ARBA00029924, ECO:0000256|HAMAP-Rule:MF_00366};
GN   Name=rpoZ {ECO:0000256|HAMAP-Rule:MF_00366};
GN   ORFNames=BN738_00630 {ECO:0000313|EMBL:CCY48808.1};
OS   Peptostreptococcus anaerobius CAG:621.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=1263100 {ECO:0000313|EMBL:CCY48808.1, ECO:0000313|Proteomes:UP000018261};
RN   [1] {ECO:0000313|EMBL:CCY48808.1, ECO:0000313|Proteomes:UP000018261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:621 {ECO:0000313|Proteomes:UP000018261};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|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:0000256|HAMAP-Rule:MF_00366}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC       {ECO:0000256|ARBA:ARBA00006711, ECO:0000256|HAMAP-Rule:MF_00366}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCY48808.1}.
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DR   EMBL; CAYH010000075; CCY48808.1; -; Genomic_DNA.
DR   RefSeq; WP_002842682.1; NZ_HF990914.1.
DR   AlphaFoldDB; R5J2K3; -.
DR   GeneID; 79841962; -.
DR   Proteomes; UP000018261; Unassembled WGS sequence.
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:DNA-templated transcription; 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   NCBIfam; TIGR00690; rpoZ; 1.
DR   PANTHER; PTHR34476; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR   PANTHER; PTHR34476:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00366};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00366}; Reference proteome {ECO:0000313|Proteomes:UP000018261};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00366}.
FT   COILED          61..88
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   88 AA;  10264 MW;  7F2A1BC9F984109A CRC64;
     MLKPSLNDIV EKIDNRYYLI ATVSKRAREI VDNSKPLIDA DEKDKPVVVA SEEIIAGKVS
     YRLLTNEEIE EKERVHKLEQ ERKLLEQE
//
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