SPXO_BACSU
ID SPXO_BACSU Reviewed; 54 AA.
AC O32302;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Anti-adapter protein SpxO {ECO:0000305};
GN Name=spxO {ECO:0000312|EMBL:CAX52691.1};
GN Synonyms=yirB {ECO:0000303|PubMed:9353931},
GN yuzO {ECO:0000303|PubMed:21378193}; OrderedLocusNames=BSU33029;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, AND INTERACTION WITH SPXH/YJBH.
RC STRAIN=168 / JH642;
RX PubMed=21378193; DOI=10.1128/jb.01350-10;
RA Kommineni S., Garg S.K., Chan C.M., Zuber P.;
RT "YjbH-enhanced proteolysis of Spx by ClpXP in Bacillus subtilis is
RT inhibited by the small protein YirB (YuzO).";
RL J. Bacteriol. 193:2133-2140(2011).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30001325; DOI=10.1371/journal.pgen.1007531;
RA Rojas-Tapias D.F., Helmann J.D.;
RT "Stabilization of Bacillus subtilis Spx under cell wall stress requires the
RT anti-adaptor protein YirB.";
RL PLoS Genet. 14:e1007531-e1007531(2018).
CC -!- FUNCTION: Inhibitor of Spx proteolytic control. Acts by interacting
CC with SpxH/YjbH, which disrups interaction between SpxH and Spx, and
CC inhibits SpxH-enhanced proteolysis of Spx by ClpXP (PubMed:21378193).
CC Required for the stabilization of Spx and activation of Spx-regulated
CC genes in response to cell wall stress (PubMed:30001325).
CC {ECO:0000269|PubMed:21378193, ECO:0000269|PubMed:30001325}.
CC -!- SUBUNIT: Interacts with SpxH. {ECO:0000269|PubMed:21378193}.
CC -!- INTERACTION:
CC O32302; O31606: spxH; NbExp=3; IntAct=EBI-6413973, EBI-6406036;
CC -!- INDUCTION: Induced under cell wall stress, but not disulfide stress,
CC and this induction requires the CssRS two-component system, which
CC responds to both secretion stress and cell wall antibiotics.
CC Phosphorylated CssR acts as an anti-repressor by antagonizing YuxN
CC repression. {ECO:0000269|PubMed:30001325}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene causes a decrease in the
CC overall Spx levels, as well as a change in the dynamics of Spx
CC accumulation. {ECO:0000269|PubMed:30001325}.
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DR EMBL; Z93941; CAB07975.1; -; Genomic_DNA.
DR EMBL; AL009126; CAX52691.1; -; Genomic_DNA.
DR RefSeq; WP_003221681.1; NZ_JNCM01000033.1.
DR RefSeq; YP_003097785.1; NC_000964.3.
DR AlphaFoldDB; O32302; -.
DR SMR; O32302; -.
DR IntAct; O32302; 1.
DR STRING; 224308.BSU33029; -.
DR PaxDb; O32302; -.
DR PRIDE; O32302; -.
DR EnsemblBacteria; CAX52691; CAX52691; BSU_33029.
DR GeneID; 50136154; -.
DR GeneID; 64305059; -.
DR GeneID; 8303202; -.
DR KEGG; bsu:BSU33029; -.
DR PATRIC; fig|224308.179.peg.3579; -.
DR eggNOG; ENOG5030DN8; Bacteria.
DR OMA; ICEKKWV; -.
DR BioCyc; BSUB:BSU33029-MON; -.
DR PRO; PR:O32302; -.
DR Proteomes; UP000001570; Chromosome.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..54
FT /note="Anti-adapter protein SpxO"
FT /id="PRO_0000382897"
SQ SEQUENCE 54 AA; 6620 MW; 5A8CF96B635300E5 CRC64;
MRELDEMISR LRNRGIKVEK VKYPKQTLSE KKWVHQCKQP LKTNYRDFNG YSFT
