ID   LOLB_PSEP1              Reviewed;         205 AA.
AC   A5VYG2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Pput_0758;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ76922.1; -; Genomic_DNA.
DR   RefSeq; WP_003247402.1; NC_009512.1.
DR   AlphaFoldDB; A5VYG2; -.
DR   SMR; A5VYG2; -.
DR   STRING; 351746.Pput_0758; -.
DR   EnsemblBacteria; ABQ76922; ABQ76922; Pput_0758.
DR   KEGG; ppf:Pput_0758; -.
DR   eggNOG; COG3017; Bacteria.
DR   HOGENOM; CLU_092816_2_1_6; -.
DR   OMA; YQTRGSF; -.
DR   OrthoDB; 1797257at2; -.
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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   CHAIN           18..205
FT                   /note="Outer-membrane lipoprotein LolB"
FT                   /id="PRO_1000021670"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ   SEQUENCE   205 AA;  22913 MW;  0E7AED63CEF205B2 CRC64;
     MFLRHCITFT MIALLAGCAG FGSREALQGH GDPQQWRAHK AQLSSLDGWQ INGKVGIRAP
     RDSGSGTLFW LQRQDYYDIR LAGPLGRGAA RLTGRPGGVV LEVANQGRYE ATSPEALLEE
     QLGWQLPVSH LVWWVRGLPA PDSKSKLTLD GDSRLASLDQ DGWQVQYLSY TEQNGYWLPE
     RLKLHGKDLD VTLVVKDWQP RQLGH