SCTN_SHIFL
ID SCTN_SHIFL Reviewed; 430 AA.
AC P0A1C1; P35531;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
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:26947936, ECO:0000305|PubMed:27770024};
GN Name=sctN {ECO:0000303|PubMed:9618447};
GN Synonyms=mxiB, spa47 {ECO:0000303|PubMed:1312536}, spaL;
GN OrderedLocusNames=CP0149;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pMYSH6000, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=1312536; DOI=10.1128/jb.174.6.1990-2001.1992;
RA Venkatesan M.M., Buysse J.M., Oaks E.V.;
RT "Surface presentation of Shigella flexneri invasion plasmid antigens
RT requires the products of the spa locus.";
RL J. Bacteriol. 174:1990-2001(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=8385666; DOI=10.1128/jb.175.8.2334-2346.1993;
RA Sasakawa C., Komatsu K., Tobe T., Suzuki T., Yoshikawa M.;
RT "Eight genes in region 5 that form an operon are essential for invasion of
RT epithelial cells by Shigella flexneri 2a.";
RL J. Bacteriol. 175:2334-2346(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [6]
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 [7]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH MXIN/SCTL AND MXIK/SCTK.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=12864857; DOI=10.1046/j.1365-2958.2003.03590.x;
RA Jouihri N., Sory M.P., Page A.L., Gounon P., Parsot C., Allaoui A.;
RT "MxiK and MxiN interact with the Spa47 ATPase and are required for transit
RT of the needle components MxiH and MxiI, but not of Ipa proteins, through
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 49:755-767(2003).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH SPA33/SCTQ; MXIN/SCTL
RP AND MXIK/SCTK.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=18657109; DOI=10.1111/j.1574-6968.2008.01284.x;
RA Johnson S., Blocker A.;
RT "Characterization of soluble complexes of the Shigella flexneri type III
RT secretion system ATPase.";
RL FEMS Microbiol. Lett. 286:274-278(2008).
RN [9]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH MXIN/SCTL AND
RP SPA13/SCTO.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=25583506; DOI=10.1073/pnas.1411610112;
RA Hu B., Morado D.R., Margolin W., Rohde J.R., Arizmendi O., Picking W.L.,
RA Picking W.D., Liu J.;
RT "Visualization of the type III secretion sorting platform of Shigella
RT flexneri.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1047-1052(2015).
RN [10]
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-165.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=26947936; DOI=10.1002/pro.2917;
RA Burgess J.L., Jones H.B., Kumar P., Toth R.T. IV, Middaugh C.R., Antony E.,
RA Dickenson N.E.;
RT "Spa47 is an oligomerization-activated type three secretion system (T3SS)
RT ATPase from Shigella flexneri.";
RL Protein Sci. 25:1037-1048(2016).
RN [11]
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INTERACTION WITH MXIN/SCTL, DOMAIN, AND MUTAGENESIS OF
RP 1-MET--THR-79 AND 1-MET--LEU-6.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=29595954; DOI=10.1021/acs.biochem.8b00070;
RA Case H.B., Dickenson N.E.;
RT "MxiN differentially regulates monomeric and oligomeric species of the
RT Shigella type three secretion system ATPase Spa47.";
RL Biochemistry 57:2266-2277(2018).
RN [12]
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).
RN [13]
RP ACTIVITY REGULATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=31978132; DOI=10.1371/journal.pone.0228227;
RA Burgess J.L., Case H.B., Burgess R.A., Dickenson N.E.;
RT "Dominant negative effects by inactive Spa47 mutants inhibit T3SS function
RT and Shigella virulence.";
RL PLoS ONE 15:e0228227-e0228227(2020).
RN [14] {ECO:0007744|PDB:5SWJ, ECO:0007744|PDB:5SWL, ECO:0007744|PDB:5SYP, ECO:0007744|PDB:5SYR}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 80-430 OF WILD-TYPE AND MUTANTS
RP ALA-165; ALA-188 AND ALA-350, FUNCTION, ATPASE ACTIVITY, ACTIVITY
RP REGULATION, DOMAIN, AND MUTAGENESIS OF 1-MET--THR-79; LYS-165; GLU-188 AND
RP ARG-350.
RX PubMed=27770024; DOI=10.1074/jbc.m116.755256;
RA Burgess J.L., Burgess R.A., Morales Y., Bouvang J.M., Johnson S.J.,
RA Dickenson N.E.;
RT "Structural and biochemical characterization of Spa47 provides mechanistic
RT insight into type III secretion system ATPase activation and Shigella
RT virulence regulation.";
RL J. Biol. Chem. 291:25837-25852(2016).
RN [15] {ECO:0007744|PDB:5YBH, ECO:0007744|PDB:5YBI, ECO:0007744|PDB:5ZT1}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 84-430 IN COMPLEXES WITH ATP
RP ANALOGS AND MAGNESIUM, ATPASE ACTIVITY, DOMAIN, AND MUTAGENESIS OF CYS-163;
RP LYS-165; PHE-167; ASP-249; LEU-305; LEU-306; GLU-307; ASP-308; ASP-310;
RP PHE-311; ASP-313 AND ARG-350.
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=30013545; DOI=10.3389/fmicb.2018.01468;
RA Gao X., Mu Z., Yu X., Qin B., Wojdyla J., Wang M., Cui S.;
RT "Structural insight into conformational changes induced by ATP binding in a
RT type III secretion-associated ATPase from Shigella flexneri.";
RL Front. Microbiol. 9:1468-1468(2018).
RN [16] {ECO:0007744|PDB:6N6L, ECO:0007744|PDB:6N6M, ECO:0007744|PDB:6N6Z, ECO:0007744|PDB:6N70, ECO:0007744|PDB:6N71, ECO:0007744|PDB:6N72, ECO:0007744|PDB:6N73, ECO:0007744|PDB:6N74, ECO:0007744|PDB:6N75, ECO:0007744|PDB:6N76}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 80-430 OF MUTANTS, FUNCTION,
RP ATPASE ACTIVITY, AND MUTAGENESIS OF ARG-189; ARG-191; GLU-267; ARG-271;
RP ARG-272 AND GLU-287.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=31162724; DOI=10.1002/prot.25754;
RA Demler H.J., Case H.B., Morales Y., Bernard A.R., Johnson S.J.,
RA Dickenson N.E.;
RT "Interfacial amino acids support Spa47 oligomerization and shigella type
RT three secretion system activation.";
RL Proteins 87:931-942(2019).
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:26947936, PubMed:27770024,
CC PubMed:29595954). Acts as a molecular motor to provide the energy that
CC is required for the export of proteins (Probable). Required for type
CC III secretion apparatus (T3SA) formation, proper protein secretion,
CC host cell invasion and virulence (PubMed:26947936, PubMed:27770024,
CC PubMed:31162724). 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:0000269|PubMed:26947936, ECO:0000269|PubMed:27770024,
CC ECO:0000269|PubMed:29595954, ECO:0000269|PubMed:31162724,
CC ECO:0000305|PubMed:26947936, ECO:0000305|PubMed:27770024}.
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:26947936, ECO:0000305|PubMed:27770024};
CC -!- ACTIVITY REGULATION: Oligomerization increases ATPase activity
CC (PubMed:26947936, PubMed:27770024, PubMed:29595954, PubMed:31978132).
CC Monomeric forms exhibit low-level ATPase activity by forming short-
CC lived oligomers with active site contributions from at least two
CC protomers. In contrast, oligomers exhibit enhanced ATP hydrolysis rates
CC that likely result from multiple preformed active sites within the
CC oligomeric complex (PubMed:31978132). Oligomerization is important for
CC both enzyme activation and T3SS function (PubMed:31978132). Activity is
CC regulated by MxiN/SctL, which differentially regulates the activity of
CC the monomer and the oligomer: it up-regulates the ATPase activity of
CC the monomer, while it down-regulates the activity of the oligomer
CC (PubMed:29595954). {ECO:0000269|PubMed:26947936,
CC ECO:0000269|PubMed:27770024, ECO:0000269|PubMed:29595954,
CC ECO:0000269|PubMed:31978132}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=181 uM for ATP (monomeric form) {ECO:0000269|PubMed:29595954};
CC KM=114 uM for ATP (trimeric form) {ECO:0000269|PubMed:29595954};
CC KM=201 uM for ATP (monomeric form, in the presence of MxiN/SctL)
CC {ECO:0000269|PubMed:29595954};
CC KM=116 uM for ATP (trimeric form, in the presence of MxiN/SctL)
CC {ECO:0000269|PubMed:29595954};
CC Vmax=0.28 umol/min/mg enzyme for ATPase activity (monomeric form)
CC {ECO:0000269|PubMed:29595954};
CC Vmax=1.04 umol/min/mg enzyme for ATPase activity (trimeric form)
CC {ECO:0000269|PubMed:29595954};
CC Vmax=0.51 umol/min/mg enzyme for ATPase activity (monomeric form, in
CC the presence of MxiN/SctL) {ECO:0000269|PubMed:29595954};
CC Vmax=0.62 umol/min/mg enzyme for ATPase activity (trimeric form, in
CC the presence of MxiN/SctL) {ECO:0000269|PubMed:29595954};
CC Note=kcat is 0.22 sec(-1) for ATPase activity (monomeric form). kcat
CC is 0.84 sec(-1) for ATPase activity (trimeric form). kcat is 0.41
CC sec(-1) for ATPase activity (monomeric form, in the presence of
CC MxiN/SctL). kcat is 0.50 sec(-1) for ATPase activity (trimeric form,
CC in the presence of MxiN/SctL). {ECO:0000269|PubMed:29595954};
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:25583506). This subunit is part of the cytosolic complex
CC (PubMed:18657109, PubMed:25583506). Forms homohexamers
CC (PubMed:25583506). Interacts directly with MxiN/SctL (stator protein)
CC and Spa13/SctO (stalk protein) (PubMed:25583506, PubMed:29595954). Can
CC form a soluble complex with Spa33/SctQ, MxiN/SctL and MxiK/SctK
CC (PubMed:12864857, PubMed:18657109). {ECO:0000269|PubMed:12864857,
CC ECO:0000269|PubMed:18657109, ECO:0000269|PubMed:25583506,
CC ECO:0000269|PubMed:29595954, ECO:0000269|PubMed:30107569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18657109,
CC ECO:0000269|PubMed:25583506}.
CC -!- DOMAIN: The N-terminal domain is required for oligomerization and
CC ATPase activity (PubMed:27770024, PubMed:29595954). The six N-terminal
CC residues are necessary for proper oligomer formation, though their
CC absence does not entirely preclude oligomerization (PubMed:29595954).
CC The extreme N-terminus is also required for interaction with MxiN/SctL
CC (PubMed:29595954). The N-terminal domain, not ATPase activity, is
CC responsible for localization of Spa47/SctN to the injectisome
CC (PubMed:31978132). The binding of ATP induces a conformational change
CC of a highly conserved luminal loop, facilitating ATP hydrolysis
CC (PubMed:30013545). {ECO:0000269|PubMed:27770024,
CC ECO:0000269|PubMed:29595954, ECO:0000269|PubMed:30013545,
CC ECO:0000269|PubMed:31978132}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective for assembly of the needle
CC and secretion of the translocon proteins IpaB/SctE and IpaC/SctB
CC (PubMed:12864857, PubMed:31978132). Amount of the needle filament
CC protein MxiH/SctF is greatly reduced (PubMed:12864857). T3SS effector
CC protein secretion is reduced in Shigella strains coexpressing wild-type
CC and inactive Spa47/SctN (PubMed:31978132).
CC {ECO:0000269|PubMed:12864857, ECO:0000269|PubMed:31978132}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; M81458; AAA26541.1; -; Genomic_DNA.
DR EMBL; D13663; BAA02825.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05824.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18468.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72302.1; -; Genomic_DNA.
DR PIR; C42284; C42284.
DR RefSeq; NP_085312.1; NC_002698.1.
DR RefSeq; NP_858282.1; NC_004851.1.
DR RefSeq; WP_000122616.1; NZ_WPGS01000043.1.
DR RefSeq; YP_009062506.1; NC_024996.1.
DR PDB; 5SWJ; X-ray; 2.40 A; A/B=80-430.
DR PDB; 5SWL; X-ray; 2.70 A; A/B=80-430.
DR PDB; 5SYP; X-ray; 2.15 A; A/B=80-430.
DR PDB; 5SYR; X-ray; 1.80 A; A/B=80-430.
DR PDB; 5YBH; X-ray; 2.50 A; A/B=84-430.
DR PDB; 5YBI; X-ray; 2.27 A; A/B=84-430.
DR PDB; 5ZT1; X-ray; 3.11 A; A/B=84-430.
DR PDB; 6N6L; X-ray; 2.15 A; A/B=80-430.
DR PDB; 6N6M; X-ray; 2.79 A; A/B=80-430.
DR PDB; 6N6Z; X-ray; 2.64 A; A/B=80-430.
DR PDB; 6N70; X-ray; 2.74 A; A/B=80-430.
DR PDB; 6N71; X-ray; 2.45 A; A/B=80-430.
DR PDB; 6N72; X-ray; 2.73 A; A/B=80-430.
DR PDB; 6N73; X-ray; 2.40 A; A/B=80-430.
DR PDB; 6N74; X-ray; 1.85 A; A/B=80-430.
DR PDB; 6N75; X-ray; 2.99 A; A/B=80-430.
DR PDB; 6N76; X-ray; 2.89 A; A/B=80-430.
DR PDBsum; 5SWJ; -.
DR PDBsum; 5SWL; -.
DR PDBsum; 5SYP; -.
DR PDBsum; 5SYR; -.
DR PDBsum; 5YBH; -.
DR PDBsum; 5YBI; -.
DR PDBsum; 5ZT1; -.
DR PDBsum; 6N6L; -.
DR PDBsum; 6N6M; -.
DR PDBsum; 6N6Z; -.
DR PDBsum; 6N70; -.
DR PDBsum; 6N71; -.
DR PDBsum; 6N72; -.
DR PDBsum; 6N73; -.
DR PDBsum; 6N74; -.
DR PDBsum; 6N75; -.
DR PDBsum; 6N76; -.
DR AlphaFoldDB; P0A1C1; -.
DR SMR; P0A1C1; -.
DR STRING; 198214.CP0149; -.
DR TCDB; 3.A.6.1.2; the type iii (virulence-related) secretory pathway (iiisp) family.
DR EnsemblBacteria; AAL72302; AAL72302; SF_p0149.
DR GeneID; 1237998; -.
DR KEGG; sfl:CP0149; -.
DR PATRIC; fig|198214.7.peg.5395; -.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; MDSATRF; -.
DR BRENDA; 7.1.2.2; 5712.
DR BRENDA; 7.4.2.8; 5712.
DR Proteomes; UP000001006; Plasmid pCP301.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding; Plasmid;
KW Protein transport; Reference proteome; Translocase; Transport; Virulence.
FT CHAIN 1..430
FT /note="Type 3 secretion system ATPase"
FT /id="PRO_0000144706"
FT BINDING 162..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30013545"
FT MUTAGEN 1..79
FT /note="Missing: Prevents oligomerization. Loss of ATPase
FT activity. Mutant is unable to form external MxiH/SctF
FT needles and to restore the invasion phenotype in a knockout
FT strain."
FT /evidence="ECO:0000269|PubMed:27770024,
FT ECO:0000269|PubMed:29595954"
FT MUTAGEN 1..6
FT /note="Missing: Forms mainly monomers. Shows a
FT significantly reduced yet robust rate of hydrolysis. Can
FT restore hemolysis and invasion phenotypes in a knockout
FT strain."
FT /evidence="ECO:0000269|PubMed:29595954"
FT MUTAGEN 163
FT /note="C->V: No change in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 165
FT /note="K->A: Lack of ATPase activity. Mutant is unable to
FT form external MxiH/SctF needles and to restore the invasion
FT phenotype in a knockout strain."
FT /evidence="ECO:0000269|PubMed:26947936,
FT ECO:0000269|PubMed:27770024, ECO:0000269|PubMed:30013545"
FT MUTAGEN 167
FT /note="F->A: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 188
FT /note="E->A: Lack of ATPase activity. Mutant is unable to
FT form external MxiH/SctF needles and to restore the invasion
FT phenotype in a knockout strain."
FT /evidence="ECO:0000269|PubMed:27770024"
FT MUTAGEN 189
FT /note="R->A,E: Reduces oligomerization. Lack of ATPase
FT activity. Abolishes invasion and hemolysis phenotype.
FT Cannot secrete IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 191
FT /note="R->A: Abolishes oligomerization. Lack of ATPase
FT activity. Abolishes invasion and hemolysis phenotype.
FT Cannot secrete IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 191
FT /note="R->E: Abolishes oligomerization. Lack of ATPase
FT activity. Exhibits moderate invasion and hemolysis levels.
FT Low levels of secreted IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 249
FT /note="D->E: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 267
FT /note="E->A,R: Does not affect oligomerization. Exhibits
FT ATPase activity levels similar to the monomeric form. Shows
FT at or near wild-type levels of hemolysis and invasion.
FT Increased IpaC secretion."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 271
FT /note="R->A: Abolishes oligomerization. Exhibits ATPase
FT activity levels similar to the wild-type monomeric form.
FT Shows at or near wild-type levels of hemolysis and
FT invasion. Wild-type levels of IpaC secretion."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 271
FT /note="R->E: Significantly reduces oligomerization.
FT Maintains wild-type monomer ATPase levels but shows
FT attenuated oligomer activity. Shows severely attenuated
FT levels of both invasion and hemolysis. Low levels of
FT secreted IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 272
FT /note="R->A: Abolishes oligomerization. Exhibits ATPase
FT activity levels similar to the wild-type monomeric form.
FT Shows severely attenuated levels of both invasion and
FT hemolysis. Low levels of secreted IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 272
FT /note="R->E: Significantly reduces oligomerization.
FT Maintains wild-type levels for both monomeric and
FT oligomeric species. Abolishes invasion and hemolysis
FT phenotype. Cannot secrete IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 287
FT /note="E->A: Reduces oligomerization. Lack of ATPase
FT activity. Exhibits moderate invasion and hemolysis levels.
FT Low levels of secreted IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 287
FT /note="E->R: Reduces oligomerization. Lack of ATPase
FT activity. Abolishes invasion and hemolysis phenotype. Low
FT levels of secreted IpaC."
FT /evidence="ECO:0000269|PubMed:31162724"
FT MUTAGEN 305
FT /note="L->D,A,I: Lacks ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 306
FT /note="L->A: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 307
FT /note="E->A: Slight decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 308
FT /note="D->A: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 310
FT /note="D->A: Slight decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 311
FT /note="F->A: Slight decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 313
FT /note="D->A: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:30013545"
FT MUTAGEN 350
FT /note="R->A: Lack of ATPase activity. Mutant is unable to
FT form external MxiH/SctF needles and to restore the invasion
FT phenotype in a knockout strain."
FT /evidence="ECO:0000269|PubMed:27770024,
FT ECO:0000269|PubMed:30013545"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5ZT1"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5SWJ"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6N73"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5SYP"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6N70"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:5SYR"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 358..382
FT /evidence="ECO:0007829|PDB:5SYR"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:6N6M"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 401..408
FT /evidence="ECO:0007829|PDB:5SYR"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:5SYR"
SQ SEQUENCE 430 AA; 47518 MW; 247205018BDD5B90 CRC64;
MSYTKLLTQL SFPNRISGPI LETSLSDVSI GEICNIQAGI ESNEIVARAQ VVGFHDEKTI
LSLIGNSRGL SRQTLIKPTA QFLHTQVGRG LLGAVVNPLG EVTDKFAVTD NSEILYRPVD
NAPPLYSERA AIEKPFLTGI KVIDSLLTCG EGQRMGIFAS AGCGKTFLMN MLIEHSGADI
YVIGLIGERG REVTETVDYL KNSEKKSRCV LVYATSDYSS VDRCNAAYIA TAIAEFFRTE
GHKVALFIDS LTRYARALRD VALAAGESPA RRGYPVSVFD SLPRLLERPG KLKAGGSITA
FYTVLLEDDD FADPLAEEVR SILDGHIYLS RNLAQKGQFP AIDSLKSISR VFTQVVDEKH
RIMAAAFREL LSEIEELRTI IDFGEYKPGE NASQDKIYNK ISVVESFLKQ DYRLGFTYEQ
TMELIGETIR
