ID   LOLA_YERPS              Reviewed;         202 AA.
AC   Q66CK1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=YPTB1402;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20642.1; -; Genomic_DNA.
DR   RefSeq; WP_002211338.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66CK1; -.
DR   SMR; Q66CK1; -.
DR   EnsemblBacteria; CAH20642; CAH20642; YPTB1402.
DR   GeneID; 66842163; -.
DR   KEGG; ypo:BZ17_1117; -.
DR   KEGG; yps:YPTB1402; -.
DR   PATRIC; fig|273123.14.peg.1184; -.
DR   OMA; YDPFVEQ; -.
DR   Proteomes; UP000001011; 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; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           22..202
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_5000098606"
SQ   SEQUENCE   202 AA;  22242 MW;  C0B8E7A58C88F76A CRC64;
     MKRLLVACCF LSGLISASAL ADASTDLQNR LSKVNSFHAS FSQAVTSSDG AVVQEGEGEL
     WVKRPNLFNW HMTSPDESVL ISDGETLWFY NPFVEQATAT WLKNATGNTP FMLITRNNPD
     DWKQYNVKQK GDDFELTPKS ASGNLKQFAI SVTPSGTIKS FTAVEQDGQR SAYTLKSQQS
     SVVDASKFTF TPPKGVTLDD QR