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Database: UniProt
Entry: B5F3V3_SALA4
LinkDB: B5F3V3_SALA4
Original site: B5F3V3_SALA4 
ID   B5F3V3_SALA4            Unreviewed;       252 AA.
AC   B5F3V3;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Lipoprotein {ECO:0000256|RuleBase:RU364102};
GN   OrderedLocusNames=SeAg_B2993 {ECO:0000313|EMBL:ACH50915.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH50915.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH50915.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH50915.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004459}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004459}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the YscJ lipoprotein family.
CC       {ECO:0000256|ARBA:ARBA00009509, ECO:0000256|RuleBase:RU364102}.
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DR   EMBL; CP001138; ACH50915.1; -; Genomic_DNA.
DR   RefSeq; WP_000621239.1; NC_011149.1.
DR   AlphaFoldDB; B5F3V3; -.
DR   KEGG; sea:SeAg_B2993; -.
DR   HOGENOM; CLU_073268_2_0_6; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.1530; Hypothetical protein rpa1041; 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   NCBIfam; TIGR02544; III_secr_YscJ; 1.
DR   PANTHER; PTHR30046; FLAGELLAR M-RING PROTEIN; 1.
DR   PANTHER; PTHR30046:SF3; SECRETION SYSTEM APPARATUS LIPOPROTEIN SSAJ; 1.
DR   Pfam; PF01514; YscJ_FliF; 1.
DR   PRINTS; PR01338; TYPE3OMKPROT.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|ARBA:ARBA00023237,
KW   ECO:0000256|RuleBase:RU364102};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU364102};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364102};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU364102};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364102};
KW   Transmembrane {ECO:0000256|RuleBase:RU364102};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364102}.
FT   TRANSMEM        211..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364102"
FT   DOMAIN          21..186
FT                   /note="Flagellar M-ring N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01514"
SQ   SEQUENCE   252 AA;  28240 MW;  2C1A6EC06667E256 CRC64;
     MIRRYLYTFL LVMTLAGCKD KDLLKGLDQE QANEVIAVLQ MHNIEANKID SGKLGYSITV
     AEPDFTAAVY WIKTYQLPPR PRVEIAQMFP ADSLVSSPRA EKARLYSAIE QRLEQSLQTM
     EGVLSARVHI SYDIDAGENG RPPKPVHLSA LAVYERGSPL AHQISDIKRF LKNSFADVDY
     DNISVVLSER SDAQLQAPGT PVKRNSFATS WIVLIILLSV MSAGFGVWYY KNHYARNKKG
     ITTDDKAKSS NE
//
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