NUSG_THEMA
ID NUSG_THEMA Reviewed; 353 AA.
AC P29397;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948};
GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; OrderedLocusNames=TM_0453;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=1429627; DOI=10.1016/s0021-9258(18)50016-8;
RA Liao D., Dennis P.P.;
RT "The organization and expression of essential transcription translation
RT component genes in the extremely thermophilic eubacterium Thermotoga
RT maritima.";
RL J. Biol. Chem. 267:22787-22797(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-352.
RA Stegmann C.M., Mandal A., Schweimer C., Burmann B., Roesch P., Wahl M.C.;
RT "Crystal structure of the antitermination factor Nusg from Thermotoga
RT maritima.";
RL Submitted (JUN-2010) to the PDB data bank.
RN [4]
RP STRUCTURE BY NMR, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=23415559; DOI=10.1016/j.str.2012.12.015;
RA Drogemuller J., Stegmann C.M., Mandal A., Steiner T., Burmann B.M.,
RA Gottesman M.E., Wohrl B.M., Rosch P., Wahl M.C., Schweimer K.;
RT "An autoinhibited state in the structure of Thermotoga maritima NusG.";
RL Structure 21:365-375(2013).
CC -!- FUNCTION: Participates in transcription elongation, termination and
CC antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}.
CC -!- ACTIVITY REGULATION: Regulated by autoinhibition via interaction of the
CC N-terminal and the C-terminal domains. Autoinhibition may prevent NusG
CC from interacting prematurely with other components of the transcription
CC complex or non-specific interactions with other cellular components.
CC {ECO:0000269|PubMed:23415559}.
CC -!- DOMAIN: The N-terminal domain interacts with RNAP and the C-terminal
CC domain binds either to Rho or to RpsJ (NusE). Contains an additional,
CC species-specific domain inserted into the N-terminal domain. The N-
CC terminal and C-terminal domains can interact and form a closed
CC conformation. {ECO:0000269|PubMed:23415559}.
CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP-
CC Rule:MF_00948}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z11839; CAA77858.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35536.1; ALT_INIT; Genomic_DNA.
DR PIR; F72375; F72375.
DR RefSeq; NP_228263.1; NC_000853.1.
DR RefSeq; WP_004081513.1; NZ_CP011107.1.
DR PDB; 2LQ8; NMR; -; A=1-41, A=230-353.
DR PDB; 2XHA; X-ray; 1.91 A; A/B=41-233.
DR PDB; 2XHC; X-ray; 2.45 A; A=1-352.
DR PDBsum; 2LQ8; -.
DR PDBsum; 2XHA; -.
DR PDBsum; 2XHC; -.
DR AlphaFoldDB; P29397; -.
DR SMR; P29397; -.
DR STRING; 243274.THEMA_02425; -.
DR EnsemblBacteria; AAD35536; AAD35536; TM_0453.
DR KEGG; tma:TM0453; -.
DR PATRIC; fig|243274.5.peg.459; -.
DR eggNOG; COG0250; Bacteria.
DR InParanoid; P29397; -.
DR OMA; MIMNDEF; -.
DR EvolutionaryTrace; P29397; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.70.940; -; 2.
DR HAMAP; MF_00948; NusG; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR043425; NusG-like.
DR InterPro; IPR040473; NusG_add.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR001062; Transcrpt_antiterm_NusG.
DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR30265; PTHR30265; 1.
DR PANTHER; PTHR30265:SF2; PTHR30265:SF2; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF02357; NusG; 2.
DR Pfam; PF18298; NusG_add; 1.
DR PRINTS; PR00338; NUSGTNSCPFCT.
DR SMART; SM00739; KOW; 1.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF82679; SSF82679; 2.
DR TIGRFAMs; TIGR00922; nusG; 1.
DR PROSITE; PS01014; NUSG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription;
KW Transcription antitermination; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..353
FT /note="Transcription termination/antitermination protein
FT NusG"
FT /id="PRO_0000113965"
FT DOMAIN 301..335
FT /note="KOW"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00948"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2XHC"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 89..103
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:2XHA"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 147..163
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2XHA"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2XHA"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2XHA"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2XHC"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:2XHC"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2XHC"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:2XHC"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:2XHC"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:2XHC"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2XHC"
SQ SEQUENCE 353 AA; 40327 MW; 98DCB44B2E2CABB5 CRC64;
MKKKWYIVLT MSGYEEKVKE NIEKKVEATG IKNLVGRIVI PEEVVLDATS PSERLILSPK
AKLHVNNGKD VNKGDLIAEE PPIYARRSGV IVDVKNVRKI VVETIDRKYT KTYYIPESAG
IEPGLRVGTK VKQGLPLSKN EEYICELDGK IVEIERMKKV VVQTPDGEQD VYYIPLDVFD
RDRIKKGKEV KQGEMLAEAR KFFAKVSGRV EVVDYSTRKE IRIYKTKRRK LFPGYVFVEM
IMNDEAYNFV RSVPYVMGFV SSGGQPVPVK DREMRPILRL AGLEEYEEKK KPVKVELGFK
VGDMVKIISG PFEDFAGVIK EIDPERQELK VNVTIFGRET PVVLHVSEVE KIE
