SCTG_SALCH
ID SCTG_SALCH Reviewed; 147 AA.
AC P37422; Q57KM4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 94.
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:8382333};
GN Synonyms=sctG {ECO:0000250|UniProtKB:P0CL43}; OrderedLocusNames=SCH_2832;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=SL2824;
RX PubMed=8382333; DOI=10.1111/j.1365-2958.1993.tb01100.x;
RA Altmeyer R.M., McNern J.K., Bossio J.C., Rosenshine I., Finlay B.B.,
RA Galan J.E.;
RT "Cloning and molecular characterization of a gene involved in Salmonella
RT adherence and invasion of cultured epithelial cells.";
RL Mol. Microbiol. 7:89-98(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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 (By similarity). Pilot
CC protein that is required for the proper localization of the secretin
CC InvG/SctC in the outer membrane (By similarity). Necessary for
CC efficient adherence and entry of these organisms into cultured
CC epithelial cells (PubMed:8382333). {ECO:0000250|UniProtKB:P0CL43,
CC ECO:0000269|PubMed:8382333}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P0CL43}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the InvH family. {ECO:0000305}.
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DR EMBL; Z17243; CAA78943.1; -; Genomic_DNA.
DR EMBL; AE017220; AAX66738.1; -; Genomic_DNA.
DR PIR; S28064; S28064.
DR RefSeq; WP_000715102.1; NC_006905.1.
DR AlphaFoldDB; P37422; -.
DR SMR; P37422; -.
DR EnsemblBacteria; AAX66738; AAX66738; SCH_2832.
DR KEGG; sec:SCH_2832; -.
DR HOGENOM; CLU_123343_0_0_6; -.
DR OMA; CMSLPYV; -.
DR Proteomes; UP000000538; 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 3: Inferred from homology;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; 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_0000021515"
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 CONFLICT 36
FT /note="Q -> E (in Ref. 1; CAA78943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16462 MW; 9358B146D32681B2 CRC64;
MKKFYSCLPV FLLIGCAQVP LPSSVSKPVQ QPGAQQEQLA NANSIDECQS LPYVPSDLAK
NKSLSNQNAD NSASKNSAIS SSIFCEKYKQ TKEQALTFFQ EHPQYMRSKE DEEQLMTEFK
KVLLEPGSKN LSIYQTLLSA HERLQAL