ID   LOLA_SHEFN              Reviewed;         214 AA.
AC   Q083B9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Sfri_1796;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
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   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI71646.1; -; Genomic_DNA.
DR   RefSeq; WP_011637262.1; NC_008345.1.
DR   AlphaFoldDB; Q083B9; -.
DR   SMR; Q083B9; -.
DR   STRING; 318167.Sfri_1796; -.
DR   EnsemblBacteria; ABI71646; ABI71646; Sfri_1796.
DR   KEGG; sfr:Sfri_1796; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_1_1_6; -.
DR   OMA; YDPFVEQ; -.
DR   OrthoDB; 1933827at2; -.
DR   Proteomes; UP000000684; 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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           24..214
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_5000130738"
SQ   SEQUENCE   214 AA;  23573 MW;  3B36EB924F80DB45 CRC64;
     MNKRITVLSL LLATSLSSAA AMADDATELR AKLSNIDSLH ATFSQQVTDI NSKPIQTGSG
     VFALAYPNQF YWHLTQPDES LIVADGANLW IYNPFAEEVT VMDVAQAVDA SPMALLVHRD
     EATWAKYSVT KRAVSGKSTC FDIQPKKLNS NVVAVSVCFE ASQLVKFNLT DEQGNLSQFA
     LTQQRKVKDN EANIFKFAVP DNVDIDDQRL KQAN