BTRV_BORBR
ID BTRV_BORBR Reviewed; 116 AA.
AC Q7WLU9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Putative anti-sigma factor antagonist BtrV;
GN Name=btrV; OrderedLocusNames=BB1646;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP PROTEIN SEQUENCE OF 55-59, INTERACTION, PHOSPHORYLATION AT SER-55,
RP MUTAGENESIS OF SER-55, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=16077112; DOI=10.1128/jb.187.16.5665-5676.2005;
RA Kozak N.A., Mattoo S., Foreman-Wykert A.K., Whitelegge J.P., Miller J.F.;
RT "Interactions between partner switcher orthologs BtrW and BtrV regulate
RT type III secretion in Bordetella.";
RL J. Bacteriol. 187:5665-5676(2005).
CC -!- FUNCTION: Possible positive regulator of sigma-B activity (By
CC similarity). Non-phosphorylated BtrV binds to BtrW, preventing its
CC association with an unknown partner(s) that might be sigma-B. When
CC phosphorylated, releases BtrW, which is then free to complex with and
CC inactivate its partner. Involved in type III secretion system (TTSS).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BtrW. {ECO:0000269|PubMed:16077112}.
CC -!- PTM: Phosphorylated by BtrW. Dephosphorylated by BtrU.
CC {ECO:0000269|PubMed:16077112}.
CC -!- MISCELLANEOUS: Type III secreted proteins Bsp22 and BopD accumulate
CC intracellularly instead of being secreted in cells expressing the
CC mutagenized BtrV.
CC -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC {ECO:0000305}.
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DR EMBL; BX640442; CAE32143.1; -; Genomic_DNA.
DR RefSeq; WP_003809935.1; NC_002927.3.
DR AlphaFoldDB; Q7WLU9; -.
DR SMR; Q7WLU9; -.
DR STRING; 257310.BB1646; -.
DR iPTMnet; Q7WLU9; -.
DR EnsemblBacteria; CAE32143; CAE32143; BB1646.
DR GeneID; 56479672; -.
DR GeneID; 66437749; -.
DR KEGG; bbr:BB1646; -.
DR eggNOG; COG1366; Bacteria.
DR HOGENOM; CLU_115403_9_2_4; -.
DR OMA; SYFKMFN; -.
DR OrthoDB; 1864829at2; -.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IEA:InterPro.
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 Direct protein sequencing; Phosphoprotein.
FT CHAIN 1..116
FT /note="Putative anti-sigma factor antagonist BtrV"
FT /id="PRO_0000349295"
FT DOMAIN 1..110
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 55
FT /note="Phosphoserine; by BtrW"
FT /evidence="ECO:0000269|PubMed:16077112"
FT MUTAGEN 55
FT /note="S->A,D: Absence of BtrW-catalyzed phosphorylation;
FT binds BtrW 2.5-fold more than wild-type."
FT /evidence="ECO:0000269|PubMed:16077112"
FT MUTAGEN 55
FT /note="S->D: Absence of BtrW-catalyzed phosphorylation;
FT binds BtrW 2-fold more than wild-type."
FT /evidence="ECO:0000269|PubMed:16077112"
SQ SEQUENCE 116 AA; 12634 MW; 676DC0BD6B005182 CRC64;
MKLTMDKIDG MLIACLQGVV NSANAEQLEA ELAAQVDKGE RRVVLDLGRL DYISSAGLRV
VLLVAKQLRQ VQGELVLCEL KPHVREVFEI SGFLSIFPVA NSREAAAAAF KTALPR