SCTN1_SALTY
ID SCTN1_SALTY Reviewed; 431 AA.
AC P0A1B9; P39444;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=SPI-1 type 3 secretion system ATPase {ECO:0000305};
DE Short=T3SS-1 ATPase {ECO:0000305};
DE EC=7.4.2.8 {ECO:0000305|PubMed:8045880};
DE AltName: Full=Invasion protein InvC;
GN Name=sctN1 {ECO:0000303|PubMed:31288030, ECO:0000303|PubMed:9618447};
GN Synonyms=invC {ECO:0000303|PubMed:8045880}, spaI,
GN spaL {ECO:0000303|PubMed:8404849}; OrderedLocusNames=STM2894;
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], FUNCTION, ATPASE ACTIVITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-165.
RC STRAIN=SR-11;
RX PubMed=8045880; DOI=10.1128/jb.176.15.4501-4510.1994;
RA Eichelberg K., Ginocchio C.C., Galan J.E.;
RT "Molecular and functional characterization of the Salmonella typhimurium
RT invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of
RT proteins.";
RL J. Bacteriol. 176:4501-4510(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-431.
RX PubMed=8404849; DOI=10.1002/j.1460-2075.1993.tb06056.x;
RA Groisman E.A., Ochman H.;
RT "Cognate gene clusters govern invasion of host epithelial cells by
RT Salmonella typhimurium and Shigella flexneri.";
RL EMBO J. 12:3779-3787(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-431.
RC STRAIN=SR-11;
RX PubMed=7752894; DOI=10.1111/j.1365-2958.1995.tb02218.x;
RA Collazo C., Zierler M.K., Galan J.E.;
RT "Functional analysis of the Salmonella typhimurium invasion genes invl and
RT invJ and identification of a target of the protein secretion apparatus
RT encoded in the inv locus.";
RL Mol. Microbiol. 15:25-38(1995).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=14762212; DOI=10.1093/nar/gkh219;
RA McKinney J.S., Zhang H., Kubori T., Galan J.E., Altman S.;
RT "Disruption of type III secretion in Salmonella enterica serovar
RT Typhimurium by external guide sequences.";
RL Nucleic Acids Res. 32:848-854(2004).
RN [7]
RP FUNCTION, ATPASE ACTIVITY, SUBUNIT, INTERACTION WITH ORGB/SCTL, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF VAL-28; VAL-51; GLY-164; LYS-165; ARG-189;
RP ARG-191; ARG-223 AND LEU-376.
RC STRAIN=SL1344;
RX PubMed=15060043; DOI=10.1128/jb.186.8.2402-2412.2004;
RA Akeda Y., Galan J.E.;
RT "Genetic analysis of the Salmonella enterica type III secretion-associated
RT ATPase InvC defines discrete functional domains.";
RL J. Bacteriol. 186:2402-2412(2004).
RN [8]
RP FUNCTION, INTERACTION WITH SICP-SPTP, AND MUTAGENESIS OF LEU-376.
RX PubMed=16208377; DOI=10.1038/nature03992;
RA Akeda Y., Galan J.E.;
RT "Chaperone release and unfolding of substrates in type III secretion.";
RL Nature 437:911-915(2005).
RN [9]
RP INTERACTION WITH SOPD.
RC STRAIN=SL1344;
RX PubMed=20185511; DOI=10.1099/mic.0.038117-0;
RA Boonyom R., Karavolos M.H., Bulmer D.M., Khan C.M.A.;
RT "Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD
RT involves N- and C-terminal signals and direct binding to the InvC ATPase.";
RL Microbiology 156:1805-1814(2010).
RN [10]
RP FUNCTION, ATPASE ACTIVITY, AND MUTAGENESIS OF GLU-306; GLU-308; GLU-309;
RP GLU-310; ASP-312; GLY-383; GLU-384; TYR-385 AND GLY-388.
RX PubMed=26170413; DOI=10.1128/jb.00434-15;
RA Kato J., Lefebre M., Galan J.E.;
RT "Structural features reminiscent of ATP-driven protein translocases are
RT essential for the function of a type III secretion-associated ATPase.";
RL J. Bacteriol. 197:3007-3014(2015).
RN [11]
RP SUBUNIT, INTERACTION WITH ORGB/SCTL AND INVI/SCTO, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND CRYO-ELECTRON TOMOGRAPHY.
RX PubMed=28283062; DOI=10.1016/j.cell.2017.02.022;
RA Hu B., Lara-Tejero M., Kong Q., Galan J.E., Liu J.;
RT "In situ molecular architecture of the Salmonella type III secretion
RT machine.";
RL Cell 168:1065-1074(2017).
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 SUBUNIT, AND INTERACTION WITH ORGB/SCTL.
RX PubMed=31288030; DOI=10.1016/j.jmb.2019.07.004;
RA Bernal I., Boernicke J., Heidemann J., Svergun D., Horstmann J.A.,
RA Erhardt M., Tuukkanen A., Uetrecht C., Kolbe M.;
RT "Molecular organization of soluble type III secretion system sorting
RT platform complexes.";
RL J. Mol. Biol. 431:3787-3803(2019).
RN [14] {ECO:0007744|PDB:6RAD, ECO:0007744|PDB:6RAE, ECO:0007744|PDB:6SDX}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 80-431 OF APOPROTEIN AND IN
RP COMPLEXES WITH ADP AND ATP ANALOG, DOMAIN, AND MUTAGENESIS OF
RP 1-MET--THR-79.
RX PubMed=31393998; DOI=10.1002/pro.3704;
RA Bernal I., Romermann J., Flacht L., Lunelli M., Uetrecht C., Kolbe M.;
RT "Structural analysis of ligand-bound states of the Salmonella type III
RT secretion system ATPase InvC.";
RL Protein Sci. 28:1888-1901(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:15060043, PubMed:16208377,
CC PubMed:26170413). 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:8045880, PubMed:14762212,
CC PubMed:15060043, PubMed:26170413). May play a critical role in T3SS
CC substrate recognition, disassembly of the effector/chaperone complex
CC and unfolding of the effector in an ATP-dependent manner prior to
CC secretion (PubMed:16208377). Releases the effector protein SptP from
CC the chaperone SicP in an ATP-dependent manner (PubMed:16208377).
CC {ECO:0000269|PubMed:14762212, ECO:0000269|PubMed:15060043,
CC ECO:0000269|PubMed:16208377, ECO:0000269|PubMed:26170413,
CC ECO:0000269|PubMed:8045880, ECO:0000305|PubMed:8045880}.
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:8045880};
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:28283062). This subunit is part of the cytosolic complex
CC (PubMed:15060043, PubMed:31288030, PubMed:28283062). Forms homohexamers
CC (PubMed:15060043, PubMed:28283062). Interacts directly with OrgB/SctL
CC (stator protein) and InvI/SctO (stalk protein) (PubMed:15060043,
CC PubMed:31288030, PubMed:28283062). Forms a complex with SpaO/SctQ and
CC OrgB/SctL (PubMed:31288030). Interacts with the chaperone/effector
CC protein complex SicP-SptP via its C terminus (PubMed:16208377).
CC Interacts with the effector protein SopD (PubMed:20185511).
CC {ECO:0000269|PubMed:15060043, ECO:0000269|PubMed:16208377,
CC ECO:0000269|PubMed:20185511, ECO:0000269|PubMed:28283062,
CC ECO:0000269|PubMed:30107569, ECO:0000269|PubMed:31288030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28283062,
CC ECO:0000305|PubMed:15060043}. Note=Associated with the membrane,
CC presumably through interactions with other components of the SPI-1-
CC encoded T3SS. {ECO:0000269|PubMed:15060043,
CC ECO:0000269|PubMed:28283062}.
CC -!- DOMAIN: Binding of ATP leads to conformational changes of two loops
CC located outside of the catalytic site. These changes could be critical
CC for interaction with the stalk protein InvI/SctO or with chaperone and
CC effector proteins during type III secretion.
CC {ECO:0000269|PubMed:31393998}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene affects the overall
CC stability of the cytoplasmic sorting platform (PubMed:28283062).
CC Disruption mutant is defective in its ability to enter cultured
CC epithelial cells (PubMed:8045880). {ECO:0000269|PubMed:28283062,
CC ECO:0000269|PubMed:8045880}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74038.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U08279; AAA74038.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE006468; AAL21774.1; -; Genomic_DNA.
DR EMBL; X73525; CAA51921.1; -; Genomic_DNA.
DR EMBL; U10872; AAA83429.1; -; Genomic_DNA.
DR PIR; S37304; S37304.
DR PIR; S60893; S60893.
DR RefSeq; NP_461815.1; NC_003197.2.
DR RefSeq; WP_000856766.1; NC_003197.2.
DR PDB; 6RAD; X-ray; 2.80 A; A=80-431.
DR PDB; 6RAE; X-ray; 2.05 A; A=80-431.
DR PDB; 6SDX; X-ray; 2.65 A; A=80-431.
DR PDBsum; 6RAD; -.
DR PDBsum; 6RAE; -.
DR PDBsum; 6SDX; -.
DR AlphaFoldDB; P0A1B9; -.
DR SMR; P0A1B9; -.
DR STRING; 99287.STM2894; -.
DR TCDB; 3.A.6.1.3; the type iii (virulence-related) secretory pathway (iiisp) family.
DR PaxDb; P0A1B9; -.
DR EnsemblBacteria; AAL21774; AAL21774; STM2894.
DR GeneID; 1254417; -.
DR KEGG; stm:STM2894; -.
DR PATRIC; fig|99287.12.peg.3050; -.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; MDSATRF; -.
DR PhylomeDB; P0A1B9; -.
DR BioCyc; SENT99287:STM2894-MON; -.
DR PHI-base; PHI:645; -.
DR PHI-base; PHI:8301; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
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 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;
KW Protein transport; Reference proteome; Translocase; Transport; Virulence.
FT CHAIN 1..431
FT /note="SPI-1 type 3 secretion system ATPase"
FT /id="PRO_0000144705"
FT BINDING 164..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:31393998"
FT MUTAGEN 1..79
FT /note="Missing: Exists predominantly as monomer in solution
FT and can self-associates into dimers."
FT /evidence="ECO:0000269|PubMed:31393998"
FT MUTAGEN 28
FT /note="V->M: Retains wild-type levels of ATPase activity.
FT Defective in type III secretion and invasion of cultured
FT cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 51
FT /note="V->E: Retains wild-type levels of ATPase activity.
FT Drastically impaired in its ability to associate with the
FT membrane. Defective in type III secretion and invasion of
FT cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 164
FT /note="G->C: Lack of ATPase activity. Exhibits a decreased
FT ability to form oligomers. Defective in type III secretion
FT and invasion of cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 165
FT /note="K->E: Lack of ATPase activity. Defective in type III
FT secretion and invasion of cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043,
FT ECO:0000269|PubMed:8045880"
FT MUTAGEN 189
FT /note="R->G: Lack of ATPase activity. Defective in type III
FT secretion and invasion of cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 191
FT /note="R->H: Lack of ATPase activity. Exhibits a decreased
FT ability to form oligomers. Defective in type III secretion
FT and invasion of cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 223
FT /note="R->H: Lack of ATPase activity. Defective in type III
FT secretion and invasion of cultured cells."
FT /evidence="ECO:0000269|PubMed:15060043"
FT MUTAGEN 306
FT /note="E->A: Almost completely abrogates the secretion of
FT SptP and also affects the secretion of early (InvJ/SctP)
FT and middle (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 308
FT /note="E->A: Almost completely abrogates the secretion of
FT SptP and also affects the secretion of early (InvJ/SctP)
FT and middle (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 309
FT /note="E->A: Shows a defect in the secretion of SptP but
FT not in the secretion of early (InvJ/SctP) or middle
FT (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 310
FT /note="E->A: Almost completely abrogates the secretion of
FT SptP and also affects the secretion of early (InvJ/SctP)
FT and middle (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 312
FT /note="D->A: Lack of ATPase activity. Severely defective
FT for the secretion of early (InvJ/SctP), middle (SipB/SctE)
FT and late (SptP) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 376
FT /note="L->P: Retains wild-type levels of ATPase activity.
FT Defective in type III secretion and invasion of cultured
FT cells. Does not bind the SicP-SptP complex."
FT /evidence="ECO:0000269|PubMed:15060043,
FT ECO:0000269|PubMed:16208377"
FT MUTAGEN 383
FT /note="G->A: Shows a defect in the secretion of SptP but
FT not in the secretion of early (InvJ/SctP) or middle
FT (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 384
FT /note="E->A: Almost completely abrogates the secretion of
FT SptP and also affects the secretion of early (InvJ/SctP)
FT and middle (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 385
FT /note="Y->A: Can still secrete the T3SS components early
FT substrates (InvJ/SctP), middle substrates (SipB/SctE,
FT SipC/SctB and SipD/SctA), but shows a marked defect in the
FT secretion of the effector proteins SptP and SopB (late
FT substrates). Secretion of the effectors SipA and SopE2 is
FT only marginally reduced."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 385
FT /note="Y->E: Almost completely abrogates the secretion of
FT SptP and also affects the secretion of early (InvJ/SctP)
FT and middle (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 385
FT /note="Y->F,W: Does not alter function."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 385
FT /note="Y->H,R,S: Shows a defect in the secretion of SptP
FT but not in the secretion of early (InvJ/SctP) or middle
FT (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT MUTAGEN 388
FT /note="G->A: Shows a defect in the secretion of SptP but
FT not in the secretion of early (InvJ/SctP) or middle
FT (SipB/SctE) substrates."
FT /evidence="ECO:0000269|PubMed:26170413"
FT CONFLICT 62
FT /note="S -> T (in Ref. 1; AAA74038)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="A -> C (in Ref. 1; AAA74038)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="A -> G (in Ref. 1; AAA74038)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="W -> R (in Ref. 1; AAA74038 and 4; AAA83429)"
FT /evidence="ECO:0000305"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:6RAE"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 357..381
FT /evidence="ECO:0007829|PDB:6RAE"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 391..407
FT /evidence="ECO:0007829|PDB:6RAE"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:6RAE"
SQ SEQUENCE 431 AA; 47611 MW; 218BC5EF154160B7 CRC64;
MKTPRLLQYL AYPQKITGPI IEAELRDVAI GELCEIRRGW HQKQVVARAQ VVGLQRERTV
LSLIGNAQGL SRDVVLYPTG RALSAWVGYS VLGAVLDPTG KIVERFTPEV APISEERVID
VAPPSYASRV GVREPLITGV RAIDGLLTCG VGQRMGIFAS AGCGKTMLMH MLIEQTEADV
FVIGLIGERG REVTEFVDML RASHKKEKCV LVFATSDFPS VDRCNAAQLA TTVAEYFRDQ
GKRVVLFIDS MTRYARALRD VALASGERPA RRGYPASVFD NLPRLLERPG ATSEGSITAF
YTVLLESEEE ADPMADEIRS ILDGHLYLSR KLAGQGHYPA IDVLKSVSRV FGQVTTPTHA
EQASAVRKLM TRLEELQLFI DLGEYRPGEN IDNDRAMQMR DSLKAWLCQP VAQYSSFDDT
LSGMNAFADQ N
