ID A0A117LJ34_9BACT Unreviewed; 411 AA.
AC A0A117LJ34;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN ORFNames=XD75_0002 {ECO:0000313|EMBL:KUK50150.1};
OS Parcubacteria bacterium 33_209.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1635290 {ECO:0000313|EMBL:KUK50150.1, ECO:0000313|Proteomes:UP000053180};
RN [1] {ECO:0000313|Proteomes:UP000053180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- FUNCTION: Participates in both transcription termination and
CC antitermination. {ECO:0000256|HAMAP-Rule:MF_00945}.
CC -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA-
CC dependent RNA polymerase and to nascent RNA. {ECO:0000256|HAMAP-
CC Rule:MF_00945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}.
CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000256|HAMAP-
CC Rule:MF_00945}.
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:KUK50150.1}.
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DR EMBL; LGFW01000001; KUK50150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LJ34; -.
DR PATRIC; fig|1635290.3.peg.220; -.
DR Proteomes; UP000053180; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR CDD; cd02134; KH-II_NusA_rpt1; 1.
DR CDD; cd22529; KH-II_NusA_rpt2; 1.
DR CDD; cd04455; S1_NusA; 1.
DR Gene3D; 3.30.300.20; -; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.30.1480.10; NusA, N-terminal domain; 1.
DR HAMAP; MF_00945_B; NusA_B; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR025249; KH_dom_NusA-like.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR030842; NusA_bac.
DR InterPro; IPR036555; NusA_N_sf.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR013735; TF_NusA_N.
DR InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR NCBIfam; TIGR01953; NusA; 1.
DR PANTHER; PTHR22648; TRANSCRIPTION TERMINATION FACTOR NUSA; 1.
DR PANTHER; PTHR22648:SF0; TRANSCRIPTION TERMINATION_ANTITERMINATION PROTEIN NUSA; 1.
DR Pfam; PF13184; KH_5; 1.
DR Pfam; PF08529; NusA_N; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00322; KH; 2.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 2.
DR SUPFAM; SSF69705; Transcription factor NusA, N-terminal domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00945};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00945};
KW Transcription antitermination {ECO:0000256|ARBA:ARBA00022814,
KW ECO:0000256|HAMAP-Rule:MF_00945};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00945};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW ECO:0000256|HAMAP-Rule:MF_00945}.
FT DOMAIN 182..245
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 83..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46429 MW; 407CFB96F98D3EC6 CRC64;
MDFQSFLSAI NQISEEKGLS SEKIIETVEH ALASAYKKEY AKRGQIIKAK INPKNGKTEF
SRTMLVVDDT MVYIPERAEG EEEETFKVSK SYRPTQEEVN SEEPKEDVTD RRVRYNEEKH
LLIEEAKKRG EKVEPGEEIV TILEPREDFG RIAAQTAKQV VLQKIREAEK EIVLEEYKSK
EGEIVSGIVQ RIEGSNVYFD IGKSLGVLPR EEQIRGEFYK EGQRLKLYIL RVDTTPRGPV
ILLSRSYPKL ISKLFELEVP EIQTGQLEIK SIAREPGSRT KIAVSAQSDE IDAIGSMVGQ
RGVRVTAVMS ELGGEKIDII EYDEDPIKFI LNSLSPAKIS DVIIGENNTA TVIVPQDQLS
LAIGKDGQNV RLAAKLTGWR LDIKGEGEQI DEEELDIDEE ETKEEETKEE N
//