ID   LOLA_PHOLL              Reviewed;         203 AA.
AC   Q7N6E9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Outer-membrane lipoprotein carrier protein {ECO:0000255|HAMAP-Rule:MF_00240};
DE   Flags: Precursor;
GN   Name=lolA {ECO:0000255|HAMAP-Rule:MF_00240}; OrderedLocusNames=plu1602;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Participates in the translocation of lipoproteins from the
CC       inner membrane to the outer membrane. Only forms a complex with a
CC       lipoprotein if the residue after the N-terminal Cys is not an aspartate
CC       (The Asp acts as a targeting signal to indicate that the lipoprotein
CC       should stay in the inner membrane). {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SIMILARITY: Belongs to the LolA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00240}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571864; CAE13895.1; -; Genomic_DNA.
DR   RefSeq; WP_011145898.1; NC_005126.1.
DR   AlphaFoldDB; Q7N6E9; -.
DR   SMR; Q7N6E9; -.
DR   STRING; 243265.plu1602; -.
DR   EnsemblBacteria; CAE13895; CAE13895; plu1602.
DR   GeneID; 24167023; -.
DR   KEGG; plu:plu1602; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_1_1_6; -.
DR   OMA; YDPFVEQ; -.
DR   OrthoDB; 1933827at2; -.
DR   BioCyc; PLUM243265:PLU_RS08070-MON; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042953; P:lipoprotein transport; IEA:InterPro.
DR   CDD; cd16325; LolA; 1.
DR   HAMAP; MF_00240; LolA; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
DR   InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac.
DR   PANTHER; PTHR35869; PTHR35869; 1.
DR   Pfam; PF03548; LolA; 1.
DR   SUPFAM; SSF89392; SSF89392; 1.
DR   TIGRFAMs; TIGR00547; lolA; 1.
PE   3: Inferred from homology;
KW   Chaperone; Periplasm; Protein transport; Reference proteome; Signal;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           22..203
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_0000018268"
SQ   SEQUENCE   203 AA;  22785 MW;  D87E0491C31EC177 CRC64;
     MKKLILIGCL MAGMNINVAW ANASQNLQER LGKVNSFHAS FTQTVTSDDG ATIQEGEGQL
     WVKRPNLFNW HMTSPDESVL VSDGKTLWFY NPFVEQVTAN WLKDATGNTP FMLITRNDAK
     EWSQYKISQQ GNDFELTPNN VTGNLKRFSI TVTTDGTIQK FSAIEQDGQK SAYQLKGQQN
     THVDAAKFSF TLPKGVTLDD QRQ