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Database: UniProt
Entry: A0A031JDD8_9SPHN
LinkDB: A0A031JDD8_9SPHN
Original site: A0A031JDD8_9SPHN 
ID   A0A031JDD8_9SPHN        Unreviewed;       540 AA.
AC   A0A031JDD8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=BV97_05281 {ECO:0000313|EMBL:EZP71176.1};
OS   Novosphingobium resinovorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP71176.1, ECO:0000313|Proteomes:UP000024329};
RN   [1] {ECO:0000313|EMBL:EZP71176.1, ECO:0000313|Proteomes:UP000024329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF1 {ECO:0000313|EMBL:EZP71176.1,
RC   ECO:0000313|Proteomes:UP000024329};
RA   Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT   "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL   Submitted (MAR-2014) 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:EZP71176.1}.
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DR   EMBL; JFYZ01000062; EZP71176.1; -; Genomic_DNA.
DR   RefSeq; WP_036530226.1; NZ_JFYZ01000062.1.
DR   AlphaFoldDB; A0A031JDD8; -.
DR   STRING; 158500.BES08_17675; -.
DR   PATRIC; fig|158500.4.peg.5357; -.
DR   eggNOG; COG0195; Bacteria.
DR   Proteomes; UP000024329; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW   Elongation factor {ECO:0000313|EMBL:EZP71176.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:EZP71176.1};
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          142..206
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          480..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          409..436
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        480..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  60050 MW;  2DB30688465C2206 CRC64;
     MASAISANRA ELIAIANSVA SEKMIDKSIV IEAMEEAIQK SARNRYGAEN DIRAKLDPRT
     GDLRLWRVVE VVEEVEDYFK QVDLKQAEKL QKGAALGDFI VDPLPPVDLG RIDAQSAKQV
     IFQKVRDAER DRQYEEFKDR AGEVITGVIK SVEFGHVIVN LGRAEGVIRR DQQIPREAAR
     VGERVRALVL RVERQNRGPQ IFLSRAHPDF MKRLFAQEVP EIYDGVIEIK AAARDPGSRA
     KIGVISNDSS IDPVGACVGM KGSRVQAVVQ EMQGEKIDII PWSEDTATFV VNALQPATVS
     RVVIDEEESR IEVVVPDDQL SLAIGRRGQN VRLASQLTGS QIDIMTEAES SEKRQKEFVE
     RSKMFEEELD VDETLSQLLV AEGFSELEEV AYIDAAELAN IEGFDEELAE ELQNRAQEAL
     DRREEANREA RRALGVEDAL AELPHLTEAM LVVLGKGGIK TLDDLADLAT DELIAKKRTE
     QRRRDGSVNK RSGRDEDKGG VLGEYGLTEE QGNEIIMAAR AHWFEDEPQA EEAADAESSQ
//
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