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Database: UniProt
Entry: A0A0S8C3Z6_9PROT
LinkDB: A0A0S8C3Z6_9PROT
Original site: A0A0S8C3Z6_9PROT 
ID   A0A0S8C3Z6_9PROT        Unreviewed;       494 AA.
AC   A0A0S8C3Z6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:KPK18565.1};
GN   ORFNames=AMJ67_09490 {ECO:0000313|EMBL:KPK18565.1};
OS   Betaproteobacteria bacterium SG8_41.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK18565.1, ECO:0000313|Proteomes:UP000051544};
RN   [1] {ECO:0000313|EMBL:KPK18565.1, ECO:0000313|Proteomes:UP000051544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_41 {ECO:0000313|EMBL:KPK18565.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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:KPK18565.1}.
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DR   EMBL; LJTT01000028; KPK18565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8C3Z6; -.
DR   STRING; 1703391.AMJ67_09490; -.
DR   PATRIC; fig|1703391.3.peg.3712; -.
DR   Proteomes; UP000051544; 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; PF14520; HHH_5; 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:KPK18565.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:KPK18565.1};
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          137..201
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   494 AA;  55291 MW;  CEC5763B2DF3B969 CRC64;
     MSRELLLLVD ALAREKNVDK TTVFGALELA LASATKKRFH EDVDVRVEID PMTGDYKSFR
     RWQVVPDEAI ETPAHQIALS EAVKLKSDIN LEEYVEEPLE PVEFGRIGAQ TAKQVILQKI
     RDAEREQILN DFLARKEHLV TGVIKRMERG NAIIESGRLE AMLPREQMIP KENLRVGDRV
     RAFVWKIDRA NRGPQLILSR TAPEFVTALF ELEVPELEDG LLEIRAAARD PGSRAKIAVL
     SKDRRIDPIG TCVGMRGSRV QAVTSELAGE RIDIILWAED SAQFVINALA PAEVSKIKVD
     EEARSMDIVV DEENLAQAIG RGGQNVRLAS ELTGWELNIM TREESEKKGE EEAVRVRSLF
     MEKLDVDEEV AEILVAEGFN TLEEVAYVPL PEMLEIESFD EATVNELRSR ARNALLTQAI
     VSEEQVEHDI EDLMKVEGMD NDTARMLAAK GVGTQEALAD FATDDLVELT ALDAERAKEL
     IMAARAPWFA ETNT
//
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