ID   SCTN_XANEU              Reviewed;         442 AA.
AC   P80153;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=hrpB6;
OS   Xanthomonas euvesicatoria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=456327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 75-3;
RX   PubMed=1472717; DOI=10.1094/mpmi-5-390;
RA   Fenselau S., Balbo I., Bonas U.;
RT   "Determinants of pathogenicity in Xanthomonas campestris pv. vesicatoria
RT   are related to proteins involved in secretion in bacterial pathogens of
RT   animals.";
RL   Mol. Plant Microbe Interact. 5:390-396(1992).
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; U33548; AAB08461.1; -; Genomic_DNA.
DR   EMBL; M99174; AAA27605.1; -; Genomic_DNA.
DR   RefSeq; WP_008575459.1; NZ_QFAL01000063.1.
DR   AlphaFoldDB; P80153; -.
DR   SMR; P80153; -.
DR   GeneID; 61777304; -.
DR   PATRIC; fig|456327.29.peg.3430; -.
DR   OMA; ICELRTP; -.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; 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; IPR013380; ATPase_T3SS_SCTN.
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   TIGRFAMs; TIGR02546; III_secr_ATP; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hypersensitive response elicitation;
KW   Nucleotide-binding; Protein transport; Translocase; Transport; Virulence.
FT   CHAIN           1..442
FT                   /note="Type 3 secretion system ATPase"
FT                   /id="PRO_0000144700"
FT   BINDING         173..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ   SEQUENCE   442 AA;  47710 MW;  6CE6D8B31F071E88 CRC64;
     MLAETPLLET TLERELATLA VGRRYGKVVE VVGTMLKVAG VQVSLGEVCE LRQRDGTLLQ
     RAEVVGFSRD LALLAPFGEL IGLSRETRVI GLGRPLAVPV GPALLGRVLD GLGEPSDGQG
     AIACDTWVPI QAQAPDPMRR RLIEHPMPTG VRIVDGLMTL GEGQRMGIFA AAGVGKSTLM
     GMFARGTQCD VNVIVLIGER GREVREFIEL ILGADGLARS VVVCATSDRS SIERAKAAYV
     GTAIAEYFRD RGLRVLLMMD SLTRFARAQR EIGLAAGEPP TRRGFPPSVF AELPRLLERA
     GMGESGSITA FYTVLAEDDT GSDPIAEEVR GILDGHLILS REIAAKNQYP AIDVLASLSR
     VMSQIVPYDH SQAAGRLRRL LAKYNEVETL VQVGEYRQGS DAVADEAIDR IDAIRDFLSQ
     PTDQLSAYEN TLELLTSVTD DA