ID   LOLA_SACD2              Reviewed;         208 AA.
AC   Q21K25;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Sde_1694;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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}.
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DR   EMBL; CP000282; ABD80954.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21K25; -.
DR   SMR; Q21K25; -.
DR   STRING; 203122.Sde_1694; -.
DR   EnsemblBacteria; ABD80954; ABD80954; Sde_1694.
DR   KEGG; sde:Sde_1694; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_0_0_6; -.
DR   OMA; YDPFVEQ; -.
DR   Proteomes; UP000001947; 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..208
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_0000336660"
SQ   SEQUENCE   208 AA;  23059 MW;  0608D9AB561A76C5 CRC64;
     MRLTKVCLVA VTMLVATVVR ADDIDALIGK LDQFNTVSGK AMQVITSADG EEIQKTESEF
     KILRPGYFYW RTLPPYEQII VSNPDTISVY DPDLEQVSIY QSEKMRNSPA SILSGNRSAI
     EKQFKVTKSG ASNDKKSTSF ELSYLDTANA DFKKLTVTFK KDQLASIVMH DMLDQVTSIT
     FGKVNTKAAL TPAQFEFTPP AGVDVIIE