ID   SCTN_SHISO              Reviewed;         430 AA.
AC   P0A1C2; P35531;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Type 3 secretion system ATPase {ECO:0000250|UniProtKB:P0A1C1};
DE            Short=T3SS ATPase {ECO:0000250|UniProtKB:P0A1C1};
DE            EC=7.4.2.8 {ECO:0000250|UniProtKB:P0A1C1};
GN   Name=sctN {ECO:0000250|UniProtKB:P0A1C1}; Synonyms=mxiB, spa47;
OS   Shigella sonnei.
OG   Plasmid pINV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HW383;
RA   Arakawa E., Kato J., Ito K., Watanabe H.;
RT   "Comparison and high conservation of nucleotide sequences of spa-mxi
RT   regions between S.sonnei and S.flexneri -- identification of a new gene
RT   coding plausible membrane protein.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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       ECO:0000250|UniProtKB:P0A1C1}.
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:P0A1C1};
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:P0A1C1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A1C1}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D50601; BAA09158.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A1C2; -.
DR   SMR; P0A1C2; -.
DR   STRING; 216599.GCA_000283715_05240; -.
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; Plasmid; Protein transport;
KW   Translocase; Transport; Virulence.
FT   CHAIN           1..430
FT                   /note="Type 3 secretion system ATPase"
FT                   /id="PRO_0000144707"
FT   BINDING         162..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ   SEQUENCE   430 AA;  47518 MW;  247205018BDD5B90 CRC64;
     MSYTKLLTQL SFPNRISGPI LETSLSDVSI GEICNIQAGI ESNEIVARAQ VVGFHDEKTI
     LSLIGNSRGL SRQTLIKPTA QFLHTQVGRG LLGAVVNPLG EVTDKFAVTD NSEILYRPVD
     NAPPLYSERA AIEKPFLTGI KVIDSLLTCG EGQRMGIFAS AGCGKTFLMN MLIEHSGADI
     YVIGLIGERG REVTETVDYL KNSEKKSRCV LVYATSDYSS VDRCNAAYIA TAIAEFFRTE
     GHKVALFIDS LTRYARALRD VALAAGESPA RRGYPVSVFD SLPRLLERPG KLKAGGSITA
     FYTVLLEDDD FADPLAEEVR SILDGHIYLS RNLAQKGQFP AIDSLKSISR VFTQVVDEKH
     RIMAAAFREL LSEIEELRTI IDFGEYKPGE NASQDKIYNK ISVVESFLKQ DYRLGFTYEQ
     TMELIGETIR