ID   LOLA_VIBCH              Reviewed;         198 AA.
AC   P57069;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Outer-membrane lipoprotein carrier protein;
DE   Flags: Precursor;
GN   Name=lolA; OrderedLocusNames=VC_1107;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LolA family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF94266.1; -; Genomic_DNA.
DR   PIR; F82241; F82241.
DR   RefSeq; NP_230752.1; NC_002505.1.
DR   RefSeq; WP_001045827.1; NZ_LT906614.1.
DR   AlphaFoldDB; P57069; -.
DR   SMR; P57069; -.
DR   STRING; 243277.VC_1107; -.
DR   DNASU; 2614377; -.
DR   EnsemblBacteria; AAF94266; AAF94266; VC_1107.
DR   GeneID; 57739784; -.
DR   KEGG; vch:VC_1107; -.
DR   PATRIC; fig|243277.26.peg.1057; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_1_1_6; -.
DR   OMA; YDPFVEQ; -.
DR   BioCyc; VCHO:VC1107-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IBA:GO_Central.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..198
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_0000018278"
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