(data stored in ACNUC9435 zone)

SWISSPROT: YSCN_YERPS

ID   YSCN_YERPS              Reviewed;         439 AA.
AC   P40291; Q663J9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   11-DEC-2019, entry version 130.
DE   RecName: Full=Probable ATP synthase YscN;
DE            EC=7.1.2.2;
DE   AltName: Full=Yop proteins secretion ATPase;
GN   Name=yscN; OrderedLocusNames=pYV0067;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pIB1, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=8169210; DOI=10.1128/jb.176.9.2619-2626.1994;
RA   Bergman T., Erickson K., Galyov E., Persson C., Wolf-Watz H.;
RT   "The lcrB (yscN/U) gene cluster of Yersinia pseudotuberculosis is involved
RT   in Yop secretion and shows high homology to the spa gene clusters of
RT   Shigella flexneri and Salmonella typhimurium.";
RL   J. Bacteriol. 176:2619-2626(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953; PLASMID=pYV;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Is a component of the Yop secretion machinery using ATP, and
CC       it is either the energizer of this machinery, or part of it.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=But connected to the inner
CC       membrane possibly through LcrD. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
DR   EMBL; U00998; AAA73398.1; -; Unassigned_DNA.
DR   EMBL; L23522; AAA20119.1; -; Unassigned_DNA.
DR   EMBL; BX936399; CAF25410.1; -; Genomic_DNA.
DR   RefSeq; WP_002212955.1; NZ_CP009711.1.
DR   SMR; P40291; -.
DR   EnsemblBacteria; CAF25410; CAF25410; pYV0067.
DR   GeneID; 39573266; -.
DR   KEGG; ypo:BZ17_4267; -.
DR   KEGG; yps:pYV0067; -.
DR   PATRIC; fig|273123.14.peg.4503; -.
DR   HOGENOM; HOG000257876; -.
DR   KO; K03224; -.
DR   OMA; FTPLCAG; -.
DR   Proteomes; UP000001011; Plasmid pYV.
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:ATPase activity; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; 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_H-transp.
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;
DR   PRODOM; P40291.
DR   SWISS-2DPAGE; P40291.
KW   ATP synthesis; ATP-binding; Cytoplasm; Hydrogen ion transport;
KW   Ion transport; Nucleotide-binding; Plasmid; Protein transport; Translocase;
KW   Transport; Virulence.
FT   CHAIN           1..439
FT                   /note="Probable ATP synthase YscN"
FT                   /id="PRO_0000144710"
FT   NP_BIND         169..176
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         169..177
FT                   /note="Missing: Abolishes ATP-binding."
FT   CONFLICT        201
FT                   /note="R -> P (in Ref. 1; AAA73398/AAA20119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="V -> F (in Ref. 1; AAA73398/AAA20119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="D -> H (in Ref. 1; AAA73398/AAA20119)"
FT                   /evidence="ECO:0000305"
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
//

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