ID   SADB_SALTY              Reviewed;         227 AA.
AC   Q8ZL65;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Inner membrane lipoprotein SadB {ECO:0000305};
DE   Flags: Precursor;
GN   Name=sadB {ECO:0000303|PubMed:24369174};
GN   OrderedLocusNames=STM3690 {ECO:0000312|EMBL:AAL22549.1};
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 [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   [2] {ECO:0007744|PDB:4C47}
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 23-227, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=24369174; DOI=10.1074/jbc.m113.513275;
RA   Grin I., Hartmann M.D., Sauer G., Hernandez Alvarez B., Schuetz M.,
RA   Wagner S., Madlung J., Macek B., Felipe-Lopez A., Hensel M., Lupas A.,
RA   Linke D.;
RT   "A trimeric lipoprotein assists in trimeric autotransporter biogenesis in
RT   enterobacteria.";
RL   J. Biol. Chem. 289:7388-7398(2014).
CC   -!- FUNCTION: Required for proper surface expression of the autotransporter
CC       adhesin SadA. Could be directly involved in the biogenesis of
CC       functionally active SadA. {ECO:0000269|PubMed:24369174}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24369174}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:24369174}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:24369174}.
CC   -!- DOMAIN: The homotrimer is held together by an extended N-terminal
CC       coiled coil, which leads into three separate globular C-terminal
CC       domains of beta-sandwich topology. {ECO:0000269|PubMed:24369174}.
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DR   EMBL; AE006468; AAL22549.1; -; Genomic_DNA.
DR   RefSeq; NP_462590.1; NC_003197.2.
DR   RefSeq; WP_000549457.1; NC_003197.2.
DR   PDB; 4C47; X-ray; 2.45 A; A/B/C=23-227.
DR   PDBsum; 4C47; -.
DR   AlphaFoldDB; Q8ZL65; -.
DR   SMR; Q8ZL65; -.
DR   STRING; 99287.STM3690; -.
DR   PaxDb; Q8ZL65; -.
DR   EnsemblBacteria; AAL22549; AAL22549; STM3690.
DR   GeneID; 1255214; -.
DR   KEGG; stm:STM3690; -.
DR   PATRIC; fig|99287.12.peg.3903; -.
DR   HOGENOM; CLU_112391_0_0_6; -.
DR   OMA; HATWGNE; -.
DR   BioCyc; SENT99287:STM3690-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.1620; -; 1.
DR   InterPro; IPR021658; DUF3251.
DR   InterPro; IPR037125; YajI-like_sf.
DR   Pfam; PF11622; DUF3251; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..227
FT                   /note="Inner membrane lipoprotein SadB"
FT                   /id="PRO_0000437737"
FT   COILED          31..68
FT                   /evidence="ECO:0000255"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   HELIX           28..91
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          111..122
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          125..134
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          144..151
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   HELIX           160..166
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          168..173
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          184..191
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:4C47"
FT   STRAND          200..206
FT                   /evidence="ECO:0007829|PDB:4C47"
SQ   SEQUENCE   227 AA;  25906 MW;  821E311C996E3A47 CRC64;
     MHKNGKFIPL LALGFTFFLS GCDYFADKHL VEEMKEQQKE QETKINLLEK QQKEQEAKIN
     LLEKQQATII NTTKKVTEVV GRVERKQRLF DYTELDPSQT HYFIINNGNI GLAGRILSIE
     PIDNGSVIHL DLVNLLSIPV SNLAFNMTWG TKKPSEAKDL PRWKQLLLNT KMDSTIELLP
     GAWTNVTLTL KGVSPNNLKY LKIGIDMENV IFDSIQPIND TKKKPKK