SCTN1_SALTI
ID SCTN1_SALTI Reviewed; 431 AA.
AC P0A1C0; P39444;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=SPI-1 type 3 secretion system ATPase {ECO:0000250|UniProtKB:P0A1B9};
DE Short=T3SS-1 ATPase {ECO:0000250|UniProtKB:P0A1B9};
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P0A1B9};
DE AltName: Full=Invasion protein InvC;
GN Name=sctN1 {ECO:0000250|UniProtKB:P0A1B9}; Synonyms=invC, spaI, spaL;
GN OrderedLocusNames=STY3017, t2796;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: ATPase component of the type III secretion system (T3SS),
CC also called injectisome, which is used to inject bacterial effector
CC proteins into eukaryotic host cells (By similarity). Acts as a
CC molecular motor to provide the energy that is required for the export
CC of proteins (By similarity). Required for type III secretion apparatus
CC (T3SA) formation, proper protein secretion, host cell invasion and
CC virulence (By similarity). May play a critical role in T3SS substrate
CC recognition, disassembly of the effector/chaperone complex and
CC unfolding of the effector in an ATP-dependent manner prior to secretion
CC (By similarity). {ECO:0000250|UniProtKB:P0A1B9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P0A1B9};
CC -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC approximately 20 different proteins, including cytoplasmic components,
CC a base, an export apparatus and a needle (By similarity). This subunit
CC is part of the cytosolic complex (By similarity). Forms homohexamers
CC (By similarity). {ECO:0000250|UniProtKB:P0A1B9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A1B9}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; AL513382; CAD06001.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70357.1; -; Genomic_DNA.
DR RefSeq; NP_457288.1; NC_003198.1.
DR RefSeq; WP_000856766.1; NZ_WSUR01000005.1.
DR AlphaFoldDB; P0A1C0; -.
DR SMR; P0A1C0; -.
DR STRING; 220341.16503972; -.
DR EnsemblBacteria; AAO70357; AAO70357; t2796.
DR KEGG; stt:t2796; -.
DR KEGG; sty:STY3017; -.
DR PATRIC; fig|220341.7.peg.3071; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; MDSATRF; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
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; SSF52540; 1.
DR TIGRFAMs; TIGR01026; fliI_yscN; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Protein transport; Translocase;
KW Transport; Virulence.
FT CHAIN 1..431
FT /note="SPI-1 type 3 secretion system ATPase"
FT /id="PRO_0000144704"
FT BINDING 162..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ SEQUENCE 431 AA; 47611 MW; 218BC5EF154160B7 CRC64;
MKTPRLLQYL AYPQKITGPI IEAELRDVAI GELCEIRRGW HQKQVVARAQ VVGLQRERTV
LSLIGNAQGL SRDVVLYPTG RALSAWVGYS VLGAVLDPTG KIVERFTPEV APISEERVID
VAPPSYASRV GVREPLITGV RAIDGLLTCG VGQRMGIFAS AGCGKTMLMH MLIEQTEADV
FVIGLIGERG REVTEFVDML RASHKKEKCV LVFATSDFPS VDRCNAAQLA TTVAEYFRDQ
GKRVVLFIDS MTRYARALRD VALASGERPA RRGYPASVFD NLPRLLERPG ATSEGSITAF
YTVLLESEEE ADPMADEIRS ILDGHLYLSR KLAGQGHYPA IDVLKSVSRV FGQVTTPTHA
EQASAVRKLM TRLEELQLFI DLGEYRPGEN IDNDRAMQMR DSLKAWLCQP VAQYSSFDDT
LSGMNAFADQ N
