SCTN_PSESM
ID SCTN_PSESM Reviewed; 449 AA.
AC Q887B5; Q9F0H7;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
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:0000250|UniProtKB:Q52371}; Synonyms=hrcN;
GN OrderedLocusNames=PSPTO_1400;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=10781092; DOI=10.1073/pnas.97.9.4856;
RA Alfano J.R., Charkowski A.O., Deng W.-L., Badel J.L., Petnicki-Ocwieja T.,
RA van Dijk K., Collmer A.;
RT "The Pseudomonas syringae Hrp pathogenicity island has a tripartite mosaic
RT structure composed of a cluster of type III secretion genes bounded by
RT exchangeable effector and conserved effector loci that contribute to
RT parasitic fitness and pathogenicity in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4856-4861(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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 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 (By similarity). This subunit
CC is part of the cytosolic complex (By similarity). Forms homododecamers
CC (By similarity). {ECO:0000250|UniProtKB:Q52371,
CC ECO:0000250|UniProtKB:Q8RK01}.
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=AAG33879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF232004; AAG33879.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016853; AAO54922.1; -; Genomic_DNA.
DR RefSeq; NP_791227.1; NC_004578.1.
DR RefSeq; WP_005763862.1; NC_004578.1.
DR AlphaFoldDB; Q887B5; -.
DR SMR; Q887B5; -.
DR STRING; 223283.PSPTO_1400; -.
DR EnsemblBacteria; AAO54922; AAO54922; PSPTO_1400.
DR GeneID; 1183036; -.
DR KEGG; pst:PSPTO_1400; -.
DR PATRIC; fig|223283.9.peg.1422; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; YKQVEML; -.
DR OrthoDB; 875807at2; -.
DR PhylomeDB; Q887B5; -.
DR Proteomes; UP000002515; 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;
KW Reference proteome; Translocase; Transport; Virulence.
FT CHAIN 1..449
FT /note="Type 3 secretion system ATPase"
FT /id="PRO_0000144702"
FT BINDING 178..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ SEQUENCE 449 AA; 48368 MW; F733EE780F86ABF1 CRC64;
MNAALNQWKD THAARLSQYS AVRVSGRVSA VRGILLECKI PAAKVGDLCE VSKADGSFLL
AEIVGFTQEC TLLSALGAPD GIQVGAPIRP LGIAHRIGVD DTLLGCVLDG FGRPLLGDCL
GAFAGPDDRR DTLPVIADAL PPTQRPRITR SLPTGIRAID SAILLGEGQR VGLFAGAGCG
KTTLMAELAR NMDCDVIVFG LIGERGRELR EFLDHELDET LRARSVLVCA TSDRSSMERA
RAAFTATAIA EAFRARGQKV LLLLDSLTRF ARAQREIGIA SGEPLGRGGL PPSVYTLLPR
LVERAGMSEN GSITALYTVL IEQDSMNDPV ADEVRSLLDG HIVLSRKLAE RGHYPAIDVS
ASISRILSNV TGRDHQRANN RLRQLLAAYK QVEMLLRLGE YQAGADPVTD CAVQLNDAIN
AFLRQDLREP VPLQETLDGL LRITSQLPE
