Y1442_THEMA
ID Y1442_THEMA Reviewed; 110 AA.
AC Q9X1F5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Putative anti-sigma factor antagonist TM_1442;
GN OrderedLocusNames=TM_1442;
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; AAD36511.1; -; Genomic_DNA.
DR PIR; G72252; G72252.
DR RefSeq; NP_229241.1; NC_000853.1.
DR RefSeq; WP_004081714.1; NZ_CP011107.1.
DR PDB; 1SBO; NMR; -; A=1-110.
DR PDB; 1T6R; NMR; -; A=1-110.
DR PDB; 1VC1; X-ray; 2.00 A; A/B=1-110.
DR PDBsum; 1SBO; -.
DR PDBsum; 1T6R; -.
DR PDBsum; 1VC1; -.
DR AlphaFoldDB; Q9X1F5; -.
DR BMRB; Q9X1F5; -.
DR SMR; Q9X1F5; -.
DR STRING; 243274.THEMA_07105; -.
DR EnsemblBacteria; AAD36511; AAD36511; TM_1442.
DR KEGG; tma:TM1442; -.
DR eggNOG; COG1366; Bacteria.
DR InParanoid; Q9X1F5; -.
DR OMA; HNSTELK; -.
DR OrthoDB; 1864829at2; -.
DR EvolutionaryTrace; Q9X1F5; -.
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..110
FT /note="Putative anti-sigma factor antagonist TM_1442"
FT /id="PRO_0000194208"
FT DOMAIN 4..110
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1VC1"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1VC1"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1VC1"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:1VC1"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1VC1"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:1VC1"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1VC1"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1VC1"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1VC1"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1VC1"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1VC1"
SQ SEQUENCE 110 AA; 12300 MW; EA1036F91820AC5D CRC64;
MNNLKLDIVE QDDKAIVRVQ GDIDAYNSSE LKEQLRNFIS TTSKKKIVLD LSSVSYMDSA
GLGTLVVILK DAKINGKEFI LSSLKESISR ILKLTHLDKI FKITDTVEEA
