SCTN2_SALTY
ID SCTN2_SALTY Reviewed; 433 AA.
AC P74857;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=SPI-2 type 3 secretion system ATPase {ECO:0000305};
DE Short=T3SS-2 ATPase {ECO:0000305};
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P0A1B9};
GN Name=sctN2 {ECO:0000303|PubMed:9618447};
GN Synonyms=ssaN {ECO:0000303|PubMed:9140973}; OrderedLocusNames=STM1415;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9140973; DOI=10.1046/j.1365-2958.1997.3271699.x;
RA Hensel M., Shea J.E., Raupach B., Monack D., Falkow S., Gleeson C.,
RA Kubo T., Holden D.W.;
RT "Functional analysis of ssaJ and the ssaK/U operon, 13 genes encoding
RT components of the type III secretion apparatus of Salmonella pathogenicity
RT island 2.";
RL Mol. Microbiol. 24:155-167(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP INTERACTION WITH T3SS-2 COMPONENTS AND T3SS-2 CHAPERONES, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-192.
RC STRAIN=SL1344;
RX PubMed=24722491; DOI=10.1371/journal.pone.0094347;
RA Yoshida Y., Miki T., Ono S., Haneda T., Ito M., Okada N.;
RT "Functional characterization of the type III secretion ATPase SsaN encoded
RT by Salmonella pathogenicity island 2.";
RL PLoS ONE 9:e94347-e94347(2014).
RN [5]
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 [6] {ECO:0007744|PDB:4NPH}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 90-433, FUNCTION, SUBUNIT,
RP INTERACTION WITH SRCA, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-379.
RX PubMed=25035427; DOI=10.1074/jbc.m114.578476;
RA Allison S.E., Tuinema B.R., Everson E.S., Sugiman-Marangos S., Zhang K.,
RA Junop M.S., Coombes B.K.;
RT "Identification of the docking site between a type III secretion system
RT ATPase and a chaperone for effector cargo.";
RL J. Biol. Chem. 289:23734-23744(2014).
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:24722491). 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, secretion of a subset of SPI-2 effectors and
CC virulence (PubMed:24722491, PubMed:25035427). May play a critical role
CC in T3SS substrate recognition, disassembly of the effector/chaperone
CC complex and unfolding of the effector in an ATP-dependent manner prior
CC to secretion (Probable). Releases the effector protein SseB from the
CC T3SS-2 specific chaperone SsaE in an ATP-dependent manner
CC (PubMed:24722491). {ECO:0000250|UniProtKB:P0A1B9,
CC ECO:0000269|PubMed:24722491, ECO:0000269|PubMed:25035427,
CC ECO:0000305|PubMed:24722491, ECO:0000305|PubMed:25035427}.
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:P0A1B9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.81 mM for ATP {ECO:0000269|PubMed:24722491};
CC Vmax=0.36 umol/min/mg enzyme for ATPase activity
CC {ECO:0000269|PubMed:24722491};
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 (PubMed:24722491). Forms
CC homohexamers (PubMed:25035427). Forms a complex with SsaK/SctL (stator
CC protein) and SsaQ/SctQ (the major sorting platform component)
CC (PubMed:24722491). Interacts with the T3SS-2 specific chaperones SsaE,
CC SseA, SscA, SscB, and SrcA (PubMed:24722491, PubMed:25035427).
CC {ECO:0000269|PubMed:24722491, ECO:0000269|PubMed:25035427,
CC ECO:0000269|PubMed:30107569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24722491}. Note=Can
CC associate with the membrane regardless of the presence of the other
CC ATPase-associated components. {ECO:0000269|PubMed:24722491}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cannot secrete the effector
CC proteins SseB, SseC, SseD, SseF, SseG and SseJ (PubMed:24722491,
CC PubMed:25035427). Mutant is also defective for the secretion of the
CC translocon proteins SseC/SctE and SseD/SctB (PubMed:25035427). Mutant
CC shows decreased virulence in the mouse model of systemic infection
CC (PubMed:24722491). {ECO:0000269|PubMed:24722491,
CC ECO:0000269|PubMed:25035427}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; Y09357; CAA70537.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20339.1; -; Genomic_DNA.
DR RefSeq; NP_460380.1; NC_003197.2.
DR RefSeq; WP_000787213.1; NC_003197.2.
DR PDB; 4NPH; X-ray; 2.09 A; A=90-433.
DR PDBsum; 4NPH; -.
DR AlphaFoldDB; P74857; -.
DR SMR; P74857; -.
DR IntAct; P74857; 6.
DR STRING; 99287.STM1415; -.
DR PaxDb; P74857; -.
DR PRIDE; P74857; -.
DR EnsemblBacteria; AAL20339; AAL20339; STM1415.
DR GeneID; 1252933; -.
DR KEGG; stm:STM1415; -.
DR PATRIC; fig|99287.12.peg.1499; -.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; ICELRTP; -.
DR PhylomeDB; P74857; -.
DR BioCyc; SENT99287:STM1415-MON; -.
DR BRENDA; 7.4.2.8; 2169.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IMP:AgBase.
DR GO; GO:0033644; C:host cell membrane; IMP:AgBase.
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; IMP:AgBase.
DR GO; GO:0051087; F:chaperone binding; IPI:AgBase.
DR GO; GO:0043621; F:protein self-association; IPI:AgBase.
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:0050714; P:positive regulation of protein secretion; IMP:AgBase.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Transport; Virulence.
FT CHAIN 1..433
FT /note="SPI-2 type 3 secretion system ATPase"
FT /id="PRO_0000144708"
FT BINDING 165..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
FT MUTAGEN 192
FT /note="R->G: Lack of ATPase activity. Cannot dissociate
FT SseB/SsaE complex."
FT /evidence="ECO:0000269|PubMed:24722491"
FT MUTAGEN 379
FT /note="V->P: Retains ATPase activity, but does not interact
FT with the chaperone SrcA. Strong virulence attenuation
FT phenotype."
FT /evidence="ECO:0000269|PubMed:25035427"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:4NPH"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 299..307
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:4NPH"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 360..384
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:4NPH"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:4NPH"
SQ SEQUENCE 433 AA; 47822 MW; 8EE0E5FCB41EA455 CRC64;
MKNELMQRLR LKYPPPDGYC RWGRIQDVSA TLLNAWLPGV FMGELCCIKP GEELAEVVGI
NGSKALLSPF TSTIGLHCGQ QVMALRRRHQ VPVGEALLGR VIDGFGRPLD GRELPDVCWK
DYDAMPPPAM VRQPITQPLM TGIRAIDSVA TCGEGQRVGI FSAPGVGKST LLAMLCNAPD
ADSNVLVLIG ERGREVREFI DFTLSEETRK RCVIVVATSD RPALERVRAL FVATTIAEFF
RDNGKRVVLL ADSLTRYARA AREIALAAGE TAVSGEYPPG VFSALPRLLE RTGMGEKGSI
TAFYTVLVEG DDMNEPLADE VRSLLDGHIV LSRRLAERGH YPAIDVLATL SRVFPVVTSH
EHRQLAAILR RCLALYQEVE LLIRIGEYQR GVDTDTDKAI DTYPDICTFL RQSKDEVCGP
ELLIEKLHQI LTE
