ID   LOLB_SALPA              Reviewed;         207 AA.
AC   Q5PCR1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Outer-membrane lipoprotein LolB {ECO:0000255|HAMAP-Rule:MF_00233};
DE   Flags: Precursor;
GN   Name=lolB {ECO:0000255|HAMAP-Rule:MF_00233}; OrderedLocusNames=SPA1095;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Plays a critical role in the incorporation of lipoproteins in
CC       the outer membrane after they are released by the LolA protein.
CC       {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00233}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SIMILARITY: Belongs to the LolB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00233}.
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DR   EMBL; CP000026; AAV77064.1; -; Genomic_DNA.
DR   RefSeq; WP_000174484.1; NC_006511.1.
DR   AlphaFoldDB; Q5PCR1; -.
DR   SMR; Q5PCR1; -.
DR   EnsemblBacteria; AAV77064; AAV77064; SPA1095.
DR   KEGG; spt:SPA1095; -.
DR   HOGENOM; CLU_092816_1_1_6; -.
DR   OMA; YQTRGSF; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd16326; LolB; 1.
DR   HAMAP; MF_00233; LolB; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR004565; OM_lipoprot_LolB.
DR   Pfam; PF03550; LolB; 1.
DR   SUPFAM; SSF89392; SSF89392; 1.
DR   TIGRFAMs; TIGR00548; lolB; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW   Protein transport; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   CHAIN           22..207
FT                   /note="Outer-membrane lipoprotein LolB"
FT                   /id="PRO_1000021677"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ   SEQUENCE   207 AA;  23686 MW;  45483A05FDA4F4DB CRC64;
     MTLPDFRLIR LLPLASLVLT ACTLPGHKGP GKSPDSPQWR QHQQEVRHLN QYQTRGAFAY
     ISDDQKVYAR FFWQQTGQDR YRLLLTNPLG STELELNAQP GNVQLVDNKG QRYTADDAEE
     MIGKLTGMPI PLNSLRQWIL GLPGDATDYK LDDQYRLSEV NYRQDGKNWK VVYGGYDSKT
     QPAMPANMEL SDGSQRIKLK MDNWIVK