ID   SCTN_YERPE              Reviewed;         439 AA.
AC   Q7ARI8; A0A0H2W055; A0A384L914; A0A3N4BJZ3; Q74YX5; Q7BTX3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Type 3 secretion system ATPase {ECO:0000303|PubMed:21611119};
DE            Short=T3SS ATPase {ECO:0000303|PubMed:21611119};
DE            EC=7.4.2.8 {ECO:0000305|PubMed:21611119};
GN   Name=sctN {ECO:0000250|UniProtKB:P40290};
GN   Synonyms=yscN {ECO:0000303|PubMed:21611119};
GN   OrderedLocusNames=YPCD1.40 {ECO:0000312|EMBL:CAB54917.1},
GN   Y0041 {ECO:0000312|EMBL:AAC69791.1};
OS   Yersinia pestis.
OG   Plasmid pCD1 {ECO:0000312|EMBL:CAB54917.1,
OG   ECO:0000312|Proteomes:UP000000815}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM5 / Biovar Mediaevalis;
RX   PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA   Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA   Blattner F.R.;
RT   "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT   Yersinia pestis KIM5.";
RL   Infect. Immun. 66:4611-4623(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM5 / Biovar Mediaevalis;
RX   PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA   Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA   Brubaker R.R., Garcia E.;
RT   "Structural organization of virulence-associated plasmids of Yersinia
RT   pestis.";
RL   J. Bacteriol. 180:5192-5202(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [4]
RP   FUNCTION, ATPASE ACTIVITY, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=21611119; DOI=10.1371/journal.pone.0019716;
RA   Swietnicki W., Carmany D., Retford M., Guelta M., Dorsey R., Bozue J.,
RA   Lee M.S., Olson M.A.;
RT   "Identification of small-molecule inhibitors of Yersinia pestis Type III
RT   secretion system YscN ATPase.";
RL   PLoS ONE 6:e19716-e19716(2011).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND IDENTIFICATION AS A POTENTIAL VACCINE.
RX   PubMed=22537022; DOI=10.1111/j.1574-6968.2012.02583.x;
RA   Bozue J., Cote C.K., Webster W., Bassett A., Tobery S., Little S.,
RA   Swietnicki W.;
RT   "A Yersinia pestis YscN ATPase mutant functions as a live attenuated
RT   vaccine against bubonic plague in mice.";
RL   FEMS Microbiol. Lett. 332:113-121(2012).
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 (PubMed:21611119). Acts as a
CC       molecular motor to provide the energy that is required for the export
CC       of proteins (Probable). 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:0000269|PubMed:21611119,
CC       ECO:0000305|PubMed:21611119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8;
CC         Evidence={ECO:0000305|PubMed:21611119};
CC   -!- ACTIVITY REGULATION: ATPase activity and YopE secretion are inhibited
CC       by selected small-molecule ATPase inhibitors.
CC       {ECO:0000269|PubMed:21611119}.
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:P40290}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40290}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect the growth
CC       rate but causes total attenuation of the pathogen in a mouse model of
CC       bubonic plague (PubMed:21611119). Deletion mutant is not able to
CC       secrete the virulence-associated V antigen (LcrV) and is attenuated in
CC       a subcutaneous model of plague (PubMed:22537022).
CC       {ECO:0000269|PubMed:21611119, ECO:0000269|PubMed:22537022}.
CC   -!- BIOTECHNOLOGY: Deletion mutant may function as an attenuated,
CC       genetically engineered, live vaccine effective against bubonic plague.
CC       Mice vaccinated twice with this mutant at varying doses are protected
CC       against bubonic plague in a dose-dependent manner.
CC       {ECO:0000269|PubMed:22537022}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF053946; AAC62564.1; -; Genomic_DNA.
DR   EMBL; AF074612; AAC69791.1; -; Genomic_DNA.
DR   EMBL; AL117189; CAB54917.1; -; Genomic_DNA.
DR   RefSeq; NP_395174.1; NC_003131.1.
DR   RefSeq; NP_857742.1; NC_004836.1.
DR   RefSeq; NP_857937.1; NC_004839.1.
DR   RefSeq; WP_002212955.1; NZ_WUCM01000070.1.
DR   AlphaFoldDB; Q7ARI8; -.
DR   SMR; Q7ARI8; -.
DR   IntAct; Q7ARI8; 5.
DR   MINT; Q7ARI8; -.
DR   STRING; 214092.5832460; -.
DR   DNASU; 1149301; -.
DR   EnsemblBacteria; PWF34652; PWF34652; DBB30_18055.
DR   GeneID; 66841108; -.
DR   KEGG; ype:YPCD1.40; -.
DR   PATRIC; fig|214092.21.peg.51; -.
DR   eggNOG; COG1157; Bacteria.
DR   HOGENOM; CLU_022398_5_1_6; -.
DR   OMA; ICELRTP; -.
DR   Proteomes; UP000000815; Plasmid pCD1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:GOC.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Plasmid; Protein transport;
KW   Reference proteome; Translocase; Transport; Virulence.
FT   CHAIN           1..439
FT                   /note="Type 3 secretion system ATPase"
FT                   /id="PRO_0000452669"
FT   BINDING         172..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ   SEQUENCE   439 AA;  47801 MW;  7CAE9B444123903E CRC64;
     MLSLDQIPHH IRHGIVGSRL IQIRGRVTQV TGTLLKAVVP GVRIGELCYL RNPDNSLSLQ
     AEVIGFAQHQ ALLIPLGEMY GISSNTEVSP TGTMHQVGVG EHLLGQVLDG LGQPFDGGHL
     PEPAAWYPVY QDAPAPMSRK LITTPLSLGI RVIDGLLTCG EGQRMGIFAA AGGGKSTLLA
     SLIRSAEVDV TVLALIGERG REVREFIESD LGEEGLRKAV LVVATSDRPS MERAKAGFVA
     TSIAEYFRDQ GKRVLLLMDS VTRFARAQRE IGLAAGEPPT RRGYPPSVFA ALPRLMERAG
     QSSKGSITAL YTVLVEGDDM TEPVADETRS ILDGHIILSR KLAAANHYPA IDVLRSASRV
     MNQIVSKEHK TWAGDLRRLL AKYEEVELLL QIGEYQKGQD KEADQAIERM GAIRGWLCQG
     THELSHFNET LNLLETLTQ