SCTN_YERPS
ID SCTN_YERPS Reviewed; 439 AA.
AC P40291; Q663J9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Type 3 secretion system ATPase {ECO:0000250|UniProtKB:P40290};
DE Short=T3SS ATPase {ECO:0000250|UniProtKB:P40290};
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P40290};
DE AltName: Full=Yop proteins secretion ATPase;
GN Name=sctN {ECO:0000303|PubMed:9618447};
GN Synonyms=yscN {ECO:0000303|PubMed:8169210}; 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).
RN [3]
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 [4]
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:P40290}.
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:P40290};
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 homohexamers (By similarity). {ECO:0000250|UniProtKB:P40290,
CC ECO:0000269|PubMed:30107569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40290}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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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 AlphaFoldDB; P40291; -.
DR SMR; P40291; -.
DR EnsemblBacteria; CAF25410; CAF25410; pYV0067.
DR GeneID; 66841108; -.
DR KEGG; ypo:BZ17_4267; -.
DR KEGG; yps:pYV0067; -.
DR PATRIC; fig|273123.14.peg.4503; -.
DR OMA; ICELRTP; -.
DR PHI-base; PHI:7902; -.
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: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: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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Plasmid; Protein transport;
KW Translocase; Transport; Virulence.
FT CHAIN 1..439
FT /note="Type 3 secretion system ATPase"
FT /id="PRO_0000144710"
FT BINDING 172..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
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
