ID SCTN_YEREN Reviewed; 439 AA.
AC P40290;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Type 3 secretion system ATPase {ECO:0000305};
DE Short=T3SS ATPase {ECO:0000305};
DE EC=7.4.2.8 {ECO:0000305|PubMed:16672607, ECO:0000305|PubMed:8132449};
DE AltName: Full=Type III secretion ATPase {ECO:0000303|PubMed:17050689};
DE AltName: Full=Yop proteins secretion ATPase;
DE AltName: Full=Ysc ATPase {ECO:0000303|PubMed:8132449};
GN Name=sctN {ECO:0000303|PubMed:25591178, ECO:0000303|PubMed:9618447};
GN Synonyms=yscN {ECO:0000303|PubMed:8132449};
OS Yersinia enterocolitica.
OG Plasmid pYVe227.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP 169-ALA--THR-177.
RC STRAIN=KNG22703 / Serotype O:9;
RX PubMed=8132449; DOI=10.1128/jb.176.6.1561-1569.1994;
RA Woestyn S., Allaoui A., Wattiau P., Cornelis G.R.;
RT "YscN, the putative energizer of the Yersinia Yop secretion machinery.";
RL J. Bacteriol. 176:1561-1569(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-150.
RX PubMed=2160939; DOI=10.1128/jb.172.6.3152-3162.1990;
RA Viitanen A.-M., Toivanen P., Skurnik M.;
RT "The lcrE gene is part of an operon in the lcr region of Yersinia
RT enterocolitica O:3.";
RL J. Bacteriol. 172:3152-3162(1990).
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 FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH YSCL/SCTL,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-175.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX PubMed=16672607; DOI=10.1128/jb.188.10.3525-3534.2006;
RA Blaylock B., Riordan K.E., Missiakas D.M., Schneewind O.;
RT "Characterization of the Yersinia enterocolitica type III secretion ATPase
RT YscN and its regulator, YscL.";
RL J. Bacteriol. 188:3525-3534(2006).
RN [5]
RP INTERACTION WITH YOPR.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX PubMed=17050689; DOI=10.1073/pnas.0605974103;
RA Sorg J.A., Blaylock B., Schneewind O.;
RT "Secretion signal recognition by YscN, the Yersinia type III secretion
RT ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16490-16495(2006).
RN [6]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=20453832; DOI=10.1038/emboj.2010.84;
RA Diepold A., Amstutz M., Abel S., Sorg I., Jenal U., Cornelis G.R.;
RT "Deciphering the assembly of the Yersinia type III secretion injectisome.";
RL EMBO J. 29:1928-1940(2010).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25591178; DOI=10.1371/journal.pbio.1002039;
RA Diepold A., Kudryashev M., Delalez N.J., Berry R.M., Armitage J.P.;
RT "Composition, formation, and regulation of the cytosolic c-ring, a dynamic
RT component of the type III secretion injectisome.";
RL PLoS Biol. 13:e1002039-e1002039(2015).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28653671; DOI=10.1038/ncomms15940;
RA Diepold A., Sezgin E., Huseyin M., Mortimer T., Eggeling C., Armitage J.P.;
RT "A dynamic and adaptive network of cytosolic interactions governs protein
RT export by the T3SS injectisome.";
RL Nat. Commun. 8:15940-15940(2017).
RN [9]
RP SUBUNIT.
RX PubMed=30101242; DOI=10.1039/c8ib00075a;
RA Rocha J.M., Richardson C.J., Zhang M., Darch C.M., Cai E., Diepold A.,
RA Gahlmann A.;
RT "Single-molecule tracking in live Yersinia enterocolitica reveals distinct
RT cytosolic complexes of injectisome subunits.";
RL Integr. Biol. (Camb.) 10:502-515(2018).
RN [10]
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 (PubMed:16672607, PubMed:8132449,
CC PubMed:20453832, PubMed:28653671). Acts as a molecular motor to provide
CC the energy that is required for the export of proteins (Probable).
CC Required for type III secretion apparatus (T3SA) formation, proper
CC protein secretion, host cell invasion and virulence (By similarity).
CC May play a critical role in T3SS substrate recognition, disassembly of
CC the effector/chaperone complex and unfolding of the effector in an ATP-
CC dependent manner prior to secretion (By similarity). Required for the
CC stabilization of the major sorting platform component (or C-ring
CC component) (PubMed:25591178). {ECO:0000250|UniProtKB:P0A1B9,
CC ECO:0000250|UniProtKB:P0A1C1, ECO:0000269|PubMed:16672607,
CC ECO:0000269|PubMed:20453832, ECO:0000269|PubMed:25591178,
CC ECO:0000269|PubMed:28653671, ECO:0000269|PubMed:8132449,
CC ECO:0000305|PubMed:16672607, ECO:0000305|PubMed:8132449}.
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:16672607, ECO:0000305|PubMed:8132449};
CC -!- ACTIVITY REGULATION: ATPase activity is negatively regulated by
CC YscL/SctL. {ECO:0000269|PubMed:16672607}.
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,
CC PubMed:20453832, PubMed:28653671, PubMed:30101242). This subunit is
CC part of the cytosolic complex (PubMed:20453832, PubMed:25591178,
CC PubMed:28653671, PubMed:30101242). Forms homohexamers
CC (PubMed:30101242). Interacts directly with YscL/SctL (stator protein)
CC (PubMed:16672607). YscN assembly requires the presence of YscC/SctC
CC (the secretin), YscJ/SctJ (the outer inner ring protein), YscQ/SctQ
CC (the major sorting platform component), YscK/SctK and YscL/SctL
CC (PubMed:20453832). Interacts with the Yersinia outer protein R (YopR)
CC in a secretion signal-dependent manner (PubMed:17050689).
CC {ECO:0000269|PubMed:16672607, ECO:0000269|PubMed:17050689,
CC ECO:0000269|PubMed:20453832, ECO:0000269|PubMed:25591178,
CC ECO:0000269|PubMed:28653671, ECO:0000269|PubMed:30101242,
CC ECO:0000269|PubMed:30107569}.
CC -!- INTERACTION:
CC P40290; Q01249: yscH; NbExp=2; IntAct=EBI-6502619, EBI-15606767;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16672607}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant secretes neither Yops nor the
CC ruler and needle subunits. {ECO:0000269|PubMed:20453832}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; AF102990; AAD16824.1; -; Genomic_DNA.
DR PIR; A55520; A55520.
DR RefSeq; NP_052401.1; NC_002120.1.
DR RefSeq; WP_010891217.1; NZ_SJZK01000009.1.
DR AlphaFoldDB; P40290; -.
DR SMR; P40290; -.
DR DIP; DIP-61297N; -.
DR IntAct; P40290; 3.
DR TCDB; 3.A.6.1.1; the type iii (virulence-related) secretory pathway (iiisp) family.
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 CDD; cd18117; ATP-synt_flagellum-secretory_path_III_N; 1.
DR CDD; cd01136; ATPase_flagellum-secretory_path_III; 1.
DR Gene3D; 3.40.50.12240; -; 1.
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 NCBIfam; TIGR01026; fliI_yscN; 1.
DR NCBIfam; TIGR02546; III_secr_ATP; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF9; SPI-1 TYPE 3 SECRETION SYSTEM ATPASE; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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_0000144709"
FT BINDING 172..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
FT MUTAGEN 169..177
FT /note="Missing: Impairs the secretion of Yop proteins."
FT /evidence="ECO:0000269|PubMed:8132449"
FT MUTAGEN 175
FT /note="K->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16672607"
SQ SEQUENCE 439 AA; 47783 MW; 7CAE9B444127D07A 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 KEADQAIERI GAIRGWLCQG
THELSHFNET LNLLETLTQ
//
