BTRW_BORBR
ID BTRW_BORBR Reviewed; 142 AA.
AC Q7WLV0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase BtrW;
DE EC=2.7.11.1;
DE AltName: Full=Anti-sigma factor;
DE AltName: Full=Sigma negative effector BtrW;
GN Name=btrW; OrderedLocusNames=BB1645;
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 FUNCTION, INTERACTION, AND MUTAGENESIS OF ASN-51; ASP-82 AND GLY-84.
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 negative regulator of sigma-B activity (By
CC similarity). Phosphorylates and inactivates its specific antagonist
CC protein, BtrV. Upon phosphorylation of BtrV, BtrW is released and binds
CC to an unknown partner(s) that might be sigma-B, thereby blocking its
CC ability to form a complex with its partner (possibly an RNA polymerase
CC holoenzyme (E-sigma-B)). Involved in type III secretion system (TTSS).
CC Phosphorylates BtrV. {ECO:0000250, ECO:0000269|PubMed:16077112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Probably able to multimerize; interacts with BtrV.
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 family. {ECO:0000305}.
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DR EMBL; BX640442; CAE32142.1; -; Genomic_DNA.
DR RefSeq; WP_003809933.1; NC_002927.3.
DR AlphaFoldDB; Q7WLV0; -.
DR SMR; Q7WLV0; -.
DR STRING; 257310.BB1645; -.
DR EnsemblBacteria; CAE32142; CAE32142; BB1645.
DR GeneID; 56479673; -.
DR KEGG; bbr:BB1645; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_24_2_4; -.
DR OMA; ADHIDYR; -.
DR OrthoDB; 1832160at2; -.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..142
FT /note="Serine/threonine-protein kinase BtrW"
FT /id="PRO_0000349294"
FT MUTAGEN 51
FT /note="N->A: Loss of kinase activity toward BtrV, enhanced
FT stability of BtrV-BtrW complexes."
FT /evidence="ECO:0000269|PubMed:16077112"
FT MUTAGEN 82
FT /note="D->A: Reduced kinase activity toward BtrV, lack of
FT stable interaction with BtrV, does not affect
FT multimerization of BtrW; when associated with A-84."
FT /evidence="ECO:0000269|PubMed:16077112"
FT MUTAGEN 84
FT /note="G->A: Reduced kinase activity toward BtrV, lack of
FT stable interaction with BtrV, does not affect
FT multimerization of BtrW; when associated with A-82."
FT /evidence="ECO:0000269|PubMed:16077112"
SQ SEQUENCE 142 AA; 15804 MW; E1E5DD3BC951886A CRC64;
MSSKTDTLEL SVTATTATDA LYWLEHIALR DRWSARLRFT LTLCADEALN NIVSHAFTPG
HPAAIHLTLR QTRREVSLHI ADNGAAYDPT QALSPPLARS LDDAQPGGHG LRLMRHFMHA
LSYQRRDGWN HLTLTSHSAP ES
