SSAJ_SALT1
ID SSAJ_SALT1 Reviewed; 249 AA.
AC D0ZWT5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Secretion system apparatus lipoprotein SsaJ;
DE Flags: Precursor;
GN Name=ssaJ; OrderedLocusNames=STM14_1705;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=12438395; DOI=10.1128/iai.70.12.7126-7135.2002;
RA Browne S.H., Lesnick M.L., Guiney D.G.;
RT "Genetic requirements for Salmonella-induced cytopathology in human
RT monocyte-derived macrophages.";
RL Infect. Immun. 70:7126-7135(2002).
CC -!- FUNCTION: Component of Salmonella pathogenicity island 2 (SPI-2) type
CC III secretion system, required for secretion of some type III-secreted
CC effectors including the SpvB exotoxin.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DISRUPTION PHENOTYPE: 25-fold reduction in cytopathic effects in human
CC monocyte-derived macrophages. {ECO:0000269|PubMed:12438395}.
CC -!- SIMILARITY: Belongs to the YscJ lipoprotein family. {ECO:0000305}.
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DR EMBL; CP001363; ACY88183.1; -; Genomic_DNA.
DR RefSeq; WP_000862874.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZWT5; -.
DR SMR; D0ZWT5; -.
DR EnsemblBacteria; ACY88183; ACY88183; STM14_1705.
DR KEGG; seo:STM14_1705; -.
DR PATRIC; fig|588858.6.peg.1639; -.
DR HOGENOM; CLU_073268_1_0_6; -.
DR OMA; GRIQQMV; -.
DR BioCyc; SENT588858:STM14_RS07900-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR003282; T3SS_HrcJ/YscJ.
DR InterPro; IPR043427; YscJ/FliF.
DR PANTHER; PTHR30046; PTHR30046; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR PRINTS; PR01338; TYPE3OMKPROT.
DR TIGRFAMs; TIGR02544; III_secr_YscJ; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Protein transport;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..249
FT /note="Secretion system apparatus lipoprotein SsaJ"
FT /id="PRO_0000410495"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 249 AA; 28521 MW; A6999389900AA641 CRC64;
MKVHRIVFLT VLTFFLTACD VDLYRSLPED EANQMLALLM QHHIDAEKKQ EEDGVTLRVE
QSQFINAVEL LRLNGYPHRQ FTTADKMFPA NQLVVSPQEE QQKINFLKEQ RIEGMLSQME
GVINAKVTIA LPTYDEGSNA SPSSVAVFIK YSPQVNMEAF RVKIKDLIEM SIPGLQYSKI
SILMQPAEFR MVADVPARQT FWIMDVINAN KGKVVKWLMK YPYPLMLSLT GLLLGVGILI
GYFCLRRRF