SCTC1_SALTY
ID SCTC1_SALTY Reviewed; 562 AA.
AC P35672;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=SPI-1 type 3 secretion system secretin {ECO:0000305};
DE Short=T3SS-1 secretin {ECO:0000305};
DE AltName: Full=Protein InvG;
DE Flags: Precursor;
GN Name=sctC1 {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000303|PubMed:9618447};
GN Synonyms=invG {ECO:0000303|PubMed:7997169}; OrderedLocusNames=STM2898;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=TML;
RX PubMed=7868245; DOI=10.1128/iai.63.3.762-769.1995;
RA Lodge J., Douce G.R., Amin I.I., Bolton A.J., Martin G.D., Chatfield S.,
RA Dougan G., Brown N.L., Stephen J.;
RT "Biological and genetic characterization of TnphoA mutants of Salmonella
RT typhimurium TML in the context of gastroenteritis.";
RL Infect. Immun. 63:762-769(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR-11;
RX PubMed=7997169; DOI=10.1111/j.1365-2958.1994.tb00450.x;
RA Kaniga K., Bossio J.C., Galan J.E.;
RT "The Salmonella typhimurium invasion genes invF and invG encode homologues
RT of the AraC and PulD family of proteins.";
RL Mol. Microbiol. 13:555-568(1994).
RN [3]
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 [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=SJW1103;
RX PubMed=9786184; DOI=10.1046/j.1365-2958.1998.01036.x;
RA Crago A.M., Koronakis V.;
RT "Salmonella InvG forms a ring-like multimer that requires the InvH
RT lipoprotein for outer membrane localization.";
RL Mol. Microbiol. 30:47-56(1998).
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 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 [7] {ECO:0007744|PDB:2Y9K}
RP STRUCTURE BY ELECTRON MICROSCOPY (8.30 ANGSTROMS) OF 34-170, FUNCTION, AND
RP SUBUNIT.
RX PubMed=21385715; DOI=10.1126/science.1199358;
RA Schraidt O., Marlovits T.C.;
RT "Three-dimensional model of Salmonella's needle complex at subnanometer
RT resolution.";
RL Science 331:1192-1195(2011).
RN [8] {ECO:0007744|PDB:3J1V, ECO:0007744|PDB:4G08}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 22-178, AND SUBUNIT.
RX PubMed=23633951; DOI=10.1371/journal.ppat.1003307;
RA Bergeron J.R., Worrall L.J., Sgourakis N.G., DiMaio F., Pfuetzner R.A.,
RA Felise H.B., Vuckovic M., Yu A.C., Miller S.I., Baker D., Strynadka N.C.;
RT "A refined model of the prototypical Salmonella SPI-1 T3SS basal body
RT reveals the molecular basis for its assembly.";
RL PLoS Pathog. 9:e1003307-e1003307(2013).
RN [9] {ECO:0007744|PDB:5TCQ, ECO:0007744|PDB:5TCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27974800; DOI=10.1038/nature20576;
RA Worrall L.J., Hong C., Vuckovic M., Deng W., Bergeron J.R.C.,
RA Majewski D.D., Huang R.K., Spreter T., Finlay B.B., Yu Z.,
RA Strynadka N.C.J.;
RT "Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome
RT basal body.";
RL Nature 540:597-601(2016).
RN [10] {ECO:0007744|PDB:6DV3, ECO:0007744|PDB:6DV6}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=30242280; DOI=10.1038/s41467-018-06298-8;
RA Hu J., Worrall L.J., Hong C., Vuckovic M., Atkinson C.E., Caveney N.,
RA Yu Z., Strynadka N.C.J.;
RT "Cryo-EM analysis of the T3S injectisome reveals the structure of the
RT needle and open secretin.";
RL Nat. Commun. 9:3840-3840(2018).
CC -!- FUNCTION: Component of the type III secretion system (T3SS), also
CC called injectisome, which is used to inject bacterial effector proteins
CC into eukaryotic host cells (PubMed:9786184, PubMed:27974800,
CC PubMed:30242280). Forms a ring-shaped multimeric structure with an
CC apparent central pore in the outer membrane (PubMed:9786184,
CC PubMed:21385715, PubMed:27974800, PubMed:30242280).
CC {ECO:0000269|PubMed:21385715, ECO:0000269|PubMed:27974800,
CC ECO:0000269|PubMed:30242280, ECO:0000269|PubMed:9786184}.
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 base, which anchors the injectisome in the
CC bacterial cell envelope (PubMed:21385715, PubMed:23633951,
CC PubMed:27974800, PubMed:30242280). Forms a stable homooligomeric
CC complex (PubMed:9786184, PubMed:21385715, PubMed:23633951,
CC PubMed:27974800, PubMed:30242280). The complex is composed of 15
CC subunits (PubMed:21385715, PubMed:23633951, PubMed:27974800).
CC {ECO:0000269|PubMed:21385715, ECO:0000269|PubMed:23633951,
CC ECO:0000269|PubMed:27974800, ECO:0000269|PubMed:30242280,
CC ECO:0000269|PubMed:9786184, ECO:0000305|PubMed:30107569}.
CC -!- INTERACTION:
CC P35672; P35672: sctC1; NbExp=2; IntAct=EBI-15771877, EBI-15771877;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02219, ECO:0000269|PubMed:27974800,
CC ECO:0000269|PubMed:9786184}. Note=Localization to the outer membrane
CC requires InvH/SctG. {ECO:0000269|PubMed:9786184}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutants are hypoinvasive in the HEp-2
CC cell assay. {ECO:0000269|PubMed:7868245}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305}.
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DR EMBL; X75302; CAA53049.1; -; Genomic_DNA.
DR EMBL; U08280; AAA74040.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21778.1; -; Genomic_DNA.
DR PIR; S54420; S54420.
DR RefSeq; NP_461819.1; NC_003197.2.
DR RefSeq; WP_000848113.1; NC_003197.2.
DR PDB; 2Y9K; EM; 8.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=34-170.
DR PDB; 3J1V; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=22-178.
DR PDB; 4G08; X-ray; 1.80 A; A=22-178.
DR PDB; 5TCQ; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-562.
DR PDB; 5TCR; EM; 6.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-562.
DR PDB; 6DV3; EM; 4.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-562.
DR PDB; 6DV6; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-562.
DR PDB; 6PEE; EM; 3.42 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P=1-562.
DR PDB; 6PEM; EM; 3.50 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q=1-562.
DR PDB; 6PEP; EM; 3.80 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q=1-562.
DR PDB; 6Q14; EM; 3.80 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q=1-562.
DR PDB; 6Q15; EM; 5.15 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q=1-562.
DR PDB; 6Q16; EM; 4.10 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q=1-562.
DR PDB; 6XFK; X-ray; 1.85 A; B=543-558.
DR PDB; 6XFL; NMR; -; B=520-562.
DR PDB; 7AH9; EM; 3.30 A; 5A/5B/5C/5D/5E/5F/5G/5H/5I/5J/5K/5L/5M/5N/5O/5P=1-562.
DR PDB; 7AHI; EM; 3.30 A; 5A/5B/5C/5D/5E/5F/5G/5H/5I/5J/5K/5L/5M/5N/5O/5P=1-562.
DR PDBsum; 2Y9K; -.
DR PDBsum; 3J1V; -.
DR PDBsum; 4G08; -.
DR PDBsum; 5TCQ; -.
DR PDBsum; 5TCR; -.
DR PDBsum; 6DV3; -.
DR PDBsum; 6DV6; -.
DR PDBsum; 6PEE; -.
DR PDBsum; 6PEM; -.
DR PDBsum; 6PEP; -.
DR PDBsum; 6Q14; -.
DR PDBsum; 6Q15; -.
DR PDBsum; 6Q16; -.
DR PDBsum; 6XFK; -.
DR PDBsum; 6XFL; -.
DR PDBsum; 7AH9; -.
DR PDBsum; 7AHI; -.
DR AlphaFoldDB; P35672; -.
DR BMRB; P35672; -.
DR SMR; P35672; -.
DR DIP; DIP-48517N; -.
DR IntAct; P35672; 2.
DR STRING; 99287.STM2898; -.
DR TCDB; 1.B.22.3.2; the outer bacterial membrane secretin (secretin) family.
DR PaxDb; P35672; -.
DR EnsemblBacteria; AAL21778; AAL21778; STM2898.
DR GeneID; 1254421; -.
DR KEGG; stm:STM2898; -.
DR PATRIC; fig|99287.12.peg.3054; -.
DR HOGENOM; CLU_022474_3_0_6; -.
DR OMA; VWYDDGA; -.
DR PhylomeDB; P35672; -.
DR BioCyc; SENT99287:STM2898-MON; -.
DR EvolutionaryTrace; P35672; -.
DR PHI-base; PHI:8730; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0030257; C:type III protein secretion system complex; IMP:CACAO.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1370.120; -; 2.
DR HAMAP; MF_02219; Type_III_secretin; 1.
DR InterPro; IPR005644; NolW-like.
DR InterPro; IPR038591; NolW-like_sf.
DR InterPro; IPR004846; T2SS/T3SS.
DR InterPro; IPR004845; T2SS_GspD_CS.
DR InterPro; IPR003522; T3SS_OM_pore_YscC.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 1.
DR PRINTS; PR01337; TYPE3OMGPROT.
DR TIGRFAMs; TIGR02516; type_III_yscC; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Protein transport;
KW Reference proteome; Signal; Translocation; Transport; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT CHAIN 25..562
FT /note="SPI-1 type 3 secretion system secretin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT /id="PRO_0000013111"
FT CONFLICT 12
FT /note="A -> R (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="E -> Q (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..205
FT /note="LRDQKMVIP -> CAIRKWLFR (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..240
FT /note="AMPAFSANG -> RCQRFQRM (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="G -> S (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..264
FT /note="AAA -> KPAEQ (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="S -> T (in Ref. 1; CAA53049 and 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="I -> V (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..380
FT /note="RPVLLTQENVP -> APGITSSGKCS (in Ref. 2; AAA74040)"
FT /evidence="ECO:0000305"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:4G08"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:4G08"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6PEE"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 303..325
FT /evidence="ECO:0007829|PDB:6PEE"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 352..376
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 381..393
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 400..412
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 450..461
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 467..483
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:6PEE"
FT STRAND 499..518
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 526..537
FT /evidence="ECO:0007829|PDB:6PEE"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:6XFK"
SQ SEQUENCE 562 AA; 61766 MW; 8022905BE256058D CRC64;
MKTHILLARV LACAALVLVT PGYSSEKIPV TGSGFVAKDD SLRTFFDAMA LQLKEPVIVS
KMAARKKITG NFEFHDPNAL LEKLSLQLGL IWYFDGQAIY IYDASEMRNA VVSLRNVSLN
EFNNFLKRSG LYNKNYPLRG DNRKGTFYVS GPPVYVDMVV NAATMMDKQN DGIELGRQKI
GVMRLNNTFV GDRTYNLRDQ KMVIPGIATA IERLLQGEEQ PLGNIVSSEP PAMPAFSANG
EKGKAANYAG GMSLQEALKQ NAAAGNIKIV AYPDTNSLLV KGTAEQVHFI EMLVKALDVA
KRHVELSLWI VDLNKSDLER LGTSWSGSIT IGDKLGVSLN QSSISTLDGS RFIAAVNALE
EKKQATVVSR PVLLTQENVP AIFDNNRTFY TKLIGERNVA LEHVTYGTMI RVLPRFSADG
QIEMSLDIED GNDKTPQSDT TTSVDALPEV GRTLISTIAR VPHGKSLLVG GYTRDANTDT
VQSIPFLGKL PLIGSLFRYS SKNKSNVVRV FMIEPKEIVD PLTPDASESV NNILKQSGAW
SGDDKLQKWV RVYLDRGQEA IK
