ID Q79GQ9_BORPE Unreviewed; 444 AA.
AC Q79GQ9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Type 3 secretion system ATPase {ECO:0000256|ARBA:ARBA00024442};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN Name=bscN {ECO:0000313|EMBL:CAE42520.1};
GN OrderedLocusNames=BP2245 {ECO:0000313|EMBL:CAE42520.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE42520.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034006};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR EMBL; BX640417; CAE42520.1; -; Genomic_DNA.
DR RefSeq; NP_880888.1; NC_002929.2.
DR RefSeq; WP_003820061.1; NZ_CP039022.1.
DR AlphaFoldDB; Q79GQ9; -.
DR STRING; 257313.BP2245; -.
DR PaxDb; 257313-BP2245; -.
DR GeneID; 69602143; -.
DR KEGG; bpe:BP2245; -.
DR PATRIC; fig|257313.5.peg.2421; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_4; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR CDD; cd18114; ATP-synt_flagellum-secretory_path_III_C; 1.
DR CDD; cd18117; ATP-synt_flagellum-secretory_path_III_N; 1.
DR CDD; cd01136; ATPase_flagellum-secretory_path_III; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR InterPro; IPR013380; ATPase_T3SS_SctN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR NCBIfam; TIGR01026; fliI_yscN; 1.
DR NCBIfam; TIGR02546; III_secr_ATP; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF9; SPI-1 TYPE 3 SECRETION SYSTEM ATPASE; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF18269; T3SS_ATPase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 163..344
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 444 AA; 48253 MW; E4EC5C2690671E12 CRC64;
MRQYHYITEM MRVALQDLST LRIKGRVVQV VGTIIKAVVP MVKIGEVCLL RNPGEDFEMH
GEVVGFVRDA ALLTPIGDMY GISSATEVIP TGRTHMVPVG PGLLGRVLDG LGRPLDAAES
GPLHAHKFYP VFADAPDPLT RRIIHAPLEL GVRVLDGLLT CGEGQRLGIF AAAGGGKSTL
LGMLVKGAAV DVTVVALIGE RGREVREFLE HELGPEGRRK SVIVCATSDK SSMERAKAAY
VATAIAEYFR DQGQRVLFLM DSVTRFARAQ REIGLAAGEP PTRRGYPPSV FATLPKLMER
AGMNQTGSIT ALYTVLVEGD DMNEPVADET RSILDGHIVL SRKLGAANHY PAVDVLASAS
RVMNAVVSPR HKYLAGRMRE LMAKYQDVEL LVKIGEYKQG ADASTDEAIQ KIGQINAFLR
QLTDEREAFE DTVLRMAEII GPES
//
