ID A3PEY1_PROM0 Unreviewed; 467 AA.
AC A3PEY1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
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:ABO18306.1};
GN OrderedLocusNames=P9301_16831 {ECO:0000313|EMBL:ABO18306.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO18306.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO18306.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO18306.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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}.
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DR EMBL; CP000576; ABO18306.1; -; Genomic_DNA.
DR RefSeq; WP_011863603.1; NC_009091.1.
DR AlphaFoldDB; A3PEY1; -.
DR STRING; 167546.P9301_16831; -.
DR KEGG; pmg:P9301_16831; -.
DR eggNOG; COG0195; Bacteria.
DR HOGENOM; CLU_029242_2_3_3; -.
DR OrthoDB; 9807233at2; -.
DR Proteomes; UP000001430; Chromosome.
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 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; 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 SMART; SM00322; KH; 2.
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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430};
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|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 263..326
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 335..412
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 410..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52640 MW; 3F2FE6DD5729E11D CRC64;
MALVILPGLN NLIEDISEEK KLPPNIVEAA LREALLKGYE KYRRTFYIGV NEDPFDEEYF
SNFDVGLDLD EEGYRILSSK IIVEEVESED HQISLIEVKQ VADDAQIGDT VVLDVTPEKE
DFGRMAASTT KQVLAQKLRD QQRKMIQEEF ADLEDPVLTA RVIRFERQSV IMGVSSGIGR
PEVEAELPKR DQLPNDNYRA NATFKVFLKE VSEIARKGPQ LFVSRANAGL VVYLFENEVP
EIQEGTVKIV AVSREANPPS RAVGPRTKVA VDSVENEVDP VGACIGARGA RIQQVVNELR
GEKIDVIKWS SDPIQYILNS LSPAKVDLVR LVDPEGQHAH VLVPPDQLSL AIGREGQNVR
LAARLTGWKI DVKNSHEYDQ EAEDAAVSEL IIQREDEEKL QREAELRLEA EQAERAAEDA
RLRELYPLPE DEEEYGEEQY EGEELTDNDP LETLQDTDIS AKEEKKR
//
