ID   LOLA_VIBC3              Reviewed;         198 AA.
AC   A5F2G9; C3LZB6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=VC0395_A0626, VC395_1122;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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; CP000627; ABQ21754.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP09132.1; -; Genomic_DNA.
DR   RefSeq; WP_001045827.1; NZ_JAACZH010000005.1.
DR   AlphaFoldDB; A5F2G9; -.
DR   SMR; A5F2G9; -.
DR   STRING; 345073.VC395_1122; -.
DR   EnsemblBacteria; ABQ21754; ABQ21754; VC0395_A0626.
DR   GeneID; 57739784; -.
DR   KEGG; vco:VC0395_A0626; -.
DR   KEGG; vcr:VC395_1122; -.
DR   PATRIC; fig|345073.21.peg.1090; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_1_1_6; -.
DR   OMA; YDPFVEQ; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           17..198
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_1000071833"
SQ   SEQUENCE   198 AA;  22301 MW;  8014685C73CD95F9 CRC64;
     MNKWLALLFC SFSAIAAPKD TLSERLAMSE GFSATFNQQV LSPEGKVILT GNGKVDIARP
     SLFRWETETP DENLLVSDGT TLWHFDPFVE QVTLYRAEEA LEQTPFVLLT RNKASDWDAY
     HVEEKGDVFT LTPTALDSNQ GRFQITISEK GVVQGFKVIE QDGQQSEFTF SKVKQQKPNA
     SVFNYKVPKG VEVDDQRN