ID   LOLA_NEIMB              Reviewed;         207 AA.
AC   P57068;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Outer-membrane lipoprotein carrier protein;
DE   Flags: Precursor;
GN   Name=lolA; OrderedLocusNames=NMB0622;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF41048.1; -; Genomic_DNA.
DR   PIR; C81178; C81178.
DR   RefSeq; NP_273666.1; NC_003112.2.
DR   RefSeq; WP_002222831.1; NC_003112.2.
DR   AlphaFoldDB; P57068; -.
DR   SMR; P57068; -.
DR   STRING; 122586.NMB0622; -.
DR   PaxDb; P57068; -.
DR   EnsemblBacteria; AAF41048; AAF41048; NMB0622.
DR   KEGG; nme:NMB0622; -.
DR   PATRIC; fig|122586.8.peg.787; -.
DR   HOGENOM; CLU_087560_0_1_4; -.
DR   OMA; YDPFVEQ; -.
DR   Proteomes; UP000000425; Chromosome.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..207
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_0000018265"
SQ   SEQUENCE   207 AA;  22284 MW;  849827D2CB0D86CA CRC64;
     MMKPHNLFQF LAVCSLTVAV ASAQAGAVDA LKQFNNDADG ISGSFTQTVQ SKKKTQTAHG
     TFKILRPGLF KWEYTKPYRQ TIVGDGQTVW LYDVDLAQVT KSSQDQAIGG SPAAILSNKT
     ALESSYTLKE DGSSNGIDYV LATPKRNNAG YQYIRIGFKG GNLAAMQLKD SFGNQTSISF
     GGLNTNPQLS RGAFKFTPPK GVDVLSN