SCTG_SALTY
ID SCTG_SALTY Reviewed; 147 AA.
AC P0CL43; P37423;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=SPI-1 type 3 secretion system pilotin {ECO:0000305};
DE AltName: Full=Invasion lipoprotein invH;
DE Flags: Precursor;
GN Name=invH {ECO:0000303|PubMed:9068645}; Synonyms=sctG {ECO:0000305};
GN OrderedLocusNames=STM2900;
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=S4194;
RX PubMed=9068645; DOI=10.1128/jb.179.6.1985-1991.1997;
RA Boyd E.F., Li J., Ochman H., Selander R.K.;
RT "Comparative genetics of the inv-spa invasion gene complex of Salmonella
RT enterica.";
RL J. Bacteriol. 179:1985-1991(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9680224; DOI=10.1046/j.1365-2958.1998.00908.x;
RA Daefler S., Russel M.;
RT "The Salmonella typhimurium InvH protein is an outer membrane lipoprotein
RT required for the proper localization of InvG.";
RL Mol. Microbiol. 28:1367-1380(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=SB300;
RX PubMed=23159244; DOI=10.1016/j.micinf.2012.10.014;
RA Pati N.B., Vishwakarma V., Jaiswal S., Periaswamy B., Hardt W.D., Suar M.;
RT "Deletion of invH gene in Salmonella enterica serovar Typhimurium limits
RT the secretion of Sip effector proteins.";
RL Microbes Infect. 15:66-73(2013).
CC -!- FUNCTION: Involved in the synthesis of the type III secretion system
CC (T3SS), also called injectisome, which is used to inject bacterial
CC effector proteins into eukaryotic host cells (PubMed:9680224,
CC PubMed:9786184). Pilot protein that is required for the proper
CC localization of the secretin InvG/SctC in the outer membrane
CC (PubMed:9680224, PubMed:9786184). Required for the secretion of the Sip
CC virulence factors (PubMed:9680224, PubMed:23159244).
CC {ECO:0000269|PubMed:23159244, ECO:0000269|PubMed:9680224,
CC ECO:0000269|PubMed:9786184}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:9680224,
CC ECO:0000269|PubMed:9786184}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:9680224}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows decreased levels of InvG/SctC
CC (PubMed:9786184). Deletion of the gene reduces the invasion efficiency
CC of the bacterium to 70-80% as compared to wild-type in vitro
CC (PubMed:23159244). SctG/invH-ssaV double mutant shows reduced secretion
CC of Sip effector proteins (SipA, SipB, SipC and SipD) (PubMed:23159244).
CC {ECO:0000269|PubMed:23159244, ECO:0000269|PubMed:9786184}.
CC -!- SIMILARITY: Belongs to the InvH family. {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; U84273; AAC45070.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21780.1; -; Genomic_DNA.
DR RefSeq; NP_461821.1; NC_003197.2.
DR RefSeq; WP_000715092.1; NC_003197.2.
DR PDB; 6XFJ; X-ray; 1.20 A; A/B/C/D=70-147.
DR PDB; 6XFK; X-ray; 1.85 A; A=84-147.
DR PDB; 6XFL; NMR; -; A=70-147.
DR PDBsum; 6XFJ; -.
DR PDBsum; 6XFK; -.
DR PDBsum; 6XFL; -.
DR AlphaFoldDB; P0CL43; -.
DR SASBDB; P0CL43; -.
DR SMR; P0CL43; -.
DR STRING; 99287.STM2900; -.
DR PaxDb; P0CL43; -.
DR EnsemblBacteria; AAL21780; AAL21780; STM2900.
DR GeneID; 1254423; -.
DR KEGG; stm:STM2900; -.
DR PATRIC; fig|99287.12.peg.3056; -.
DR HOGENOM; CLU_123343_0_0_6; -.
DR OMA; CMSLPYV; -.
DR BioCyc; SENT99287:STM2900-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR006830; InvH.
DR Pfam; PF04741; InvH; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..147
FT /note="SPI-1 type 3 secretion system pilotin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000021516"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:6XFJ"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:6XFJ"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6XFJ"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:6XFJ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6XFJ"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6XFJ"
SQ SEQUENCE 147 AA; 16455 MW; A02A407F1BC66DCF CRC64;
MKKFYSCLPV FLLIGCAQVP LPSSVSKPVQ QPGAQKEQLA NANSIDECQS LPYVPSDLAK
NKSLSNHNAD NSASKNSAIS SSIFCEKYKQ TKEQALTFFQ EHPQYMRSKE DEEQLMTEFK
KVLLEPGSKN LSIYQTLLAA HERLQAL
