ID   LOLA_SHEPC              Reviewed;         208 AA.
AC   A4Y6Z8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=Sputcn32_2010;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
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., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000681; ABP75731.1; -; Genomic_DNA.
DR   RefSeq; WP_011919316.1; NC_009438.1.
DR   AlphaFoldDB; A4Y6Z8; -.
DR   SMR; A4Y6Z8; -.
DR   STRING; 319224.Sputcn32_2010; -.
DR   GeneID; 45042468; -.
DR   KEGG; spc:Sputcn32_2010; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_1_1_6; -.
DR   OMA; YDPFVEQ; -.
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; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           23..208
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_5000241524"
SQ   SEQUENCE   208 AA;  23353 MW;  E8986057112866B4 CRC64;
     MKNLLCAVML TSPLLYSTAV FADDAQQLRN TLVNTASLKT DFKQTVTDVN KKVIQTGSGI
     LALAHPNQFY WHLTSPDESQ IVADGKDLWI YNPFAEEVVI MDFAEAINAS PIALLVHRDD
     TTWSQYSVTK KQDCYDIRPK AIDSGIVTVS VCFKNSQLTK FNVLDDKGNI SQFDLSNQKV
     ITTEDKALFK FVLPENVDID DQRLKTLN