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Database: UniProt
Entry: A0A0Q5DQL4_9BURK
LinkDB: A0A0Q5DQL4_9BURK
Original site: A0A0Q5DQL4_9BURK 
ID   A0A0Q5DQL4_9BURK        Unreviewed;       521 AA.
AC   A0A0Q5DQL4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN   Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945,
GN   ECO:0000313|EMBL:KQQ47100.1};
GN   ORFNames=ASF61_00080 {ECO:0000313|EMBL:KQQ47100.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ47100.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ47100.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47100.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ47100.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47100.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ47100.1}.
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DR   EMBL; LMNW01000001; KQQ47100.1; -; Genomic_DNA.
DR   RefSeq; WP_056149788.1; NZ_LMNW01000001.1.
DR   AlphaFoldDB; A0A0Q5DQL4; -.
DR   STRING; 1736266.ASF61_00080; -.
DR   OrthoDB; 9807233at2; -.
DR   Proteomes; UP000051032; 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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
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; IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
DR   InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR   NCBIfam; TIGR01953; NusA; 1.
DR   NCBIfam; TIGR01954; nusA_Cterm_rpt; 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; SSF47794; Rad51 N-terminal domain-like; 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   Elongation factor {ECO:0000313|EMBL:KQQ47100.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:KQQ47100.1};
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          138..202
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   521 AA;  57690 MW;  417FAC48BAEF949A CRC64;
     MSREVLLLVD ALAREKNVDK DVVFGALEFA LAQATKKRYE GEVDIRVSID RESGEFESFR
     RWHVVPDEAG LQLPDQEILH FEAKEQIPDI EVDDHIEEPI ESVEFGRRFA QDTKQVVLQR
     VRDAEREQIL ADFLERGDSL VTGTIKRMER GDAIVESGKI EARLPRDQMI PKENLRIGDR
     VRAFILRVDR NMRGPQVILS RTAPDFIAKL FELEVPEIEQ GMLEIKSAAR DAGVRAKIAV
     YTADKRIDPI GTCVGMRGSR VQAVTGELGG ERVDIVLWSD DPAQFVIGAL APANVSSIMV
     DEEKHAMDVV VDEENLAIAI GRSGQNVRLA SDLTGWKINI MTAEESADKA AQETAAVRAL
     FMEKLDVDQE VADILVEEGF ASLEEIAYVP ISEMLEIDSF DEDTVNELRT RARDALVTEA
     IASEEGLEGM EEALVGLEGM DRITAGKLGL AGIKTVEAFA GLAYDEFGAI LALSSDRARA
     LISNEFEDVT DDEMKLVDSK YDDRAKGLQA KAWTLAESAK A
//
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