ID I0JI05_HALH3 Unreviewed; 110 AA.
AC I0JI05;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Anti-sigma factor antagonist {ECO:0000256|RuleBase:RU003749};
GN Name=rsbV {ECO:0000313|EMBL:CCG43773.1};
GN OrderedLocusNames=HBHAL_1401 {ECO:0000313|EMBL:CCG43773.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG43773.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG43773.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- FUNCTION: Positive regulator of sigma-B activity. Non-phosphorylated
CC RsbV binds to RsbW, preventing its association with sigma-B. When
CC phosphorylated, releases RsbW, which is then free to complex with and
CC inactivate sigma-B. {ECO:0000256|ARBA:ARBA00024670}.
CC -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC {ECO:0000256|ARBA:ARBA00009013, ECO:0000256|RuleBase:RU003749}.
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DR EMBL; HE717023; CCG43773.1; -; Genomic_DNA.
DR RefSeq; WP_014641680.1; NC_017668.1.
DR AlphaFoldDB; I0JI05; -.
DR STRING; 866895.HBHAL_1401; -.
DR KEGG; hhd:HBHAL_1401; -.
DR PATRIC; fig|866895.3.peg.403; -.
DR eggNOG; COG1366; Bacteria.
DR HOGENOM; CLU_115403_9_3_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IEA:InterPro.
DR CDD; cd07043; STAS_anti-anti-sigma_factors; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR003658; Anti-sigma_ant.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR00377; ant_ant_sig; 1.
DR PANTHER; PTHR33495; ANTI-SIGMA FACTOR ANTAGONIST TM_1081-RELATED-RELATED; 1.
DR PANTHER; PTHR33495:SF9; ANTI-SIGMA-B FACTOR ANTAGONIST; 1.
DR Pfam; PF01740; STAS; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 3..110
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 110 AA; 12223 MW; 925B069C41EAB5DE CRC64;
MNLTIDVTNK ENIAYVVLSG EVDAFTAPKL KDALLPLTKE EGQTVEVDLQ NVNYMDSTGL
GVFISALKST KEHNTDLKLV QMQERVYRLF KITGLTEIMN IDSTVQGGMQ
//
