ID   LOLB_PECCP              Reviewed;         207 AA.
AC   C6DHY3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=PC1_2116;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT13156.1; -; Genomic_DNA.
DR   RefSeq; WP_015840347.1; NC_012917.1.
DR   AlphaFoldDB; C6DHY3; -.
DR   SMR; C6DHY3; -.
DR   STRING; 561230.PC1_2116; -.
DR   EnsemblBacteria; ACT13156; ACT13156; PC1_2116.
DR   KEGG; pct:PC1_2116; -.
DR   eggNOG; COG3017; Bacteria.
DR   HOGENOM; CLU_092816_1_1_6; -.
DR   OMA; YQTRGSF; -.
DR   OrthoDB; 1797257at2; -.
DR   Proteomes; UP000002736; 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_1000204386"
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;  23741 MW;  6FD4C4A438F6241C CRC64;
     MPTNTVRCLR LLPLASVLLA ACSVHQPTQT GKSPISPEWQ QHQQKVQQLS QYQTRGAFAY
     ISDSKRVSAN FFWQDTPPQR YRLLLTNPLG STELELRAQP DGVQITDNQG KRYVGKDAEY
     MIQQLTGMAI PLNNLRQWIL GIPGDATEFT LDERYLLKTV TYRQGNQNWN VSYQSYNTEL
     TPPLPTSLEL VQGEQRIKLK MNNWMVK