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LOLA_IDILO
ID   LOLA_IDILO              Reviewed;         200 AA.
AC   Q5R0C0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=IL0666;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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; AE017340; AAV81507.1; -; Genomic_DNA.
DR   RefSeq; WP_011233919.1; NC_006512.1.
DR   AlphaFoldDB; Q5R0C0; -.
DR   SMR; Q5R0C0; -.
DR   STRING; 283942.IL0666; -.
DR   EnsemblBacteria; AAV81507; AAV81507; IL0666.
DR   KEGG; ilo:IL0666; -.
DR   eggNOG; COG2834; Bacteria.
DR   HOGENOM; CLU_087560_0_0_6; -.
DR   OMA; YDPFVEQ; -.
DR   OrthoDB; 1933827at2; -.
DR   Proteomes; UP000001171; 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..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           19..200
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_1000005695"
SQ   SEQUENCE   200 AA;  22847 MW;  D2E0412333207A3F CRC64;
     MKAVVFAMVM AVSFNVFASG DESDKQALQS LLKQTQSLSA EFEQQVKDEQ GEVLQTLSGT
     LKLKRPANLY WHTKEPDESV MVANGKKVWY YNPFVEQVTI YAQQDMVDDS PLLLVLNSNG
     NQWQNYNVSF RDNRYFVEHQ TNGSKLELRF TDEKLTEITM VQAQGERTEL MLNNVALNET
     ISDEQFVFDV PADVDVDDQS
 
 
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