ID   SCTN_PSESY              Reviewed;         449 AA.
AC   Q52371;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Type 3 secretion system ATPase {ECO:0000250|UniProtKB:Q8RK01};
DE            Short=T3SS ATPase {ECO:0000250|UniProtKB:Q8RK01};
DE            EC=7.4.2.8 {ECO:0000250|UniProtKB:Q8RK01};
GN   Name=sctN {ECO:0000303|PubMed:9618447}; Synonyms=hrcN, hrpJ4;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Pss61;
RX   PubMed=8075421; DOI=10.1094/mpmi-7-0488;
RA   Lidell M.C., Hutcheson S.W.;
RT   "Characterization of the hrpJ and hrpU operons of Pseudomonas syringae pv.
RT   syringae Pss61: similarity with components of enteric bacteria involved in
RT   flagellar biogenesis and demonstration of their role in HarpinPss
RT   secretion.";
RL   Mol. Plant Microbe Interact. 7:488-497(1994).
RN   [2]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=9618447; DOI=10.1128/mmbr.62.2.379-433.1998;
RA   Hueck C.J.;
RT   "Type III protein secretion systems in bacterial pathogens of animals and
RT   plants.";
RL   Microbiol. Mol. Biol. Rev. 62:379-433(1998).
RN   [3]
RP   REVIEW, AND SUBUNIT.
RX   PubMed=30107569; DOI=10.1093/femsle/fny201;
RA   Wagner S., Grin I., Malmsheimer S., Singh N., Torres-Vargas C.E.,
RA   Westerhausen S.;
RT   "Bacterial type III secretion systems: a complex device for the delivery of
RT   bacterial effector proteins into eukaryotic host cells.";
RL   FEMS Microbiol. Lett. 365:0-0(2018).
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, ECO:0000250|UniProtKB:Q8RK01}.
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:Q8RK01};
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 (PubMed:30107569). This
CC       subunit is part of the cytosolic complex (By similarity). Forms
CC       homododecamers (By similarity). {ECO:0000250|UniProtKB:Q8RK01,
CC       ECO:0000269|PubMed:30107569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8RK01}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA81942.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U07346; AAA81942.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q52371; -.
DR   SMR; Q52371; -.
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; IPR001763; Rhodanese-like_dom.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Protein transport; Translocase;
KW   Transport; Virulence.
FT   CHAIN           1..449
FT                   /note="Type 3 secretion system ATPase"
FT                   /id="PRO_0000144703"
FT   BINDING         178..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ   SEQUENCE   449 AA;  48714 MW;  6B2CF3A68B0E116F CRC64;
     MNAALNLWKD AHAKRLSQYC AVRVIGRVSA VRRILLECRI PSAKVGDLCE VSKADGSLLL
     AEIVGFTQEC TLLSALGPPD GIQVGAPIRP LGVAHRIGVD DSLLGCVLDG FGRPLMGDCL
     GAFAGPEDRR TTLPVIADAL PPTQRPRITR ALPTGIRAID SAILLGEGQR VGLFAGAGCG
     KTTLMAELAR NMDCDVIVFG LIGERGRELR EFLDHELDET LRRRSVLVCA TSDRSSMERA
     RAAFTATAIA EAFRARGQKV LLLLDSLTRF ARAQREIGIA SGEPLGRGGL PPSVYTLLPR
     LVERAGMSEN GSITALYTVL IEQDSMNDPV ADEVRSLLDG HIVLSRKLAE RGHYPAIDVS
     ASISRILSNV TGRKHQRANN RLRQLLAAYK QVEMLLRLGE YQAGADPVTD CAVQLNEAIN
     AFLRQDLREP VPLQETLDRL LQLTSQLPE