Y1081_THEMA
ID Y1081_THEMA Reviewed; 113 AA.
AC Q9X0H0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Putative anti-sigma factor antagonist TM_1081;
GN OrderedLocusNames=TM_1081;
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 [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).
CC -!- FUNCTION: In the phosphorylated form it could act as an anti-anti-sigma
CC factor that counteracts an anti-sigma factor and thus releases a sigma
CC factor from inhibition. {ECO:0000250}.
CC -!- PTM: Phosphorylated on a serine residue. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36158.1; -; Genomic_DNA.
DR PIR; A72297; A72297.
DR RefSeq; NP_228887.1; NC_000853.1.
DR RefSeq; WP_004080402.1; NZ_CP011107.1.
DR PDB; 2KA5; NMR; -; A=1-113.
DR PDB; 3F43; X-ray; 1.59 A; A=1-113.
DR PDBsum; 2KA5; -.
DR PDBsum; 3F43; -.
DR AlphaFoldDB; Q9X0H0; -.
DR BMRB; Q9X0H0; -.
DR SMR; Q9X0H0; -.
DR STRING; 243274.THEMA_08950; -.
DR EnsemblBacteria; AAD36158; AAD36158; TM_1081.
DR KEGG; tma:TM1081; -.
DR eggNOG; COG1366; Bacteria.
DR InParanoid; Q9X0H0; -.
DR OMA; VVILMPN; -.
DR OrthoDB; 1864829at2; -.
DR EvolutionaryTrace; Q9X0H0; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR003658; Anti-sigma_ant.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF01740; STAS; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00377; ant_ant_sig; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..113
FT /note="Putative anti-sigma factor antagonist TM_1081"
FT /id="PRO_0000194206"
FT DOMAIN 1..110
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3F43"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3F43"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3F43"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:3F43"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3F43"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3F43"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:3F43"
SQ SEQUENCE 113 AA; 12973 MW; 88603AF80637DA4E CRC64;
MFPYKIVDDV VILMPNKELN IENAHLFKKW VFDEFLNKGY NKIFLVLSDV ESIDSFSLGV
IVNILKSISS SGGFFALVSP NEKVERVLSL TNLDRIVKIY DTISEAMEEV RRK