LOLA_XYLFT
ID LOLA_XYLFT Reviewed; 210 AA.
AC Q87DL0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=PD_0672;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO28543.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009442; AAO28543.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q87DL0; -.
DR SMR; Q87DL0; -.
DR EnsemblBacteria; AAO28543; AAO28543; PD_0672.
DR KEGG; xft:PD_0672; -.
DR HOGENOM; CLU_087560_0_0_6; -.
DR OMA; YDPFVEQ; -.
DR Proteomes; UP000002516; 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT CHAIN 24..210
FT /note="Outer-membrane lipoprotein carrier protein"
FT /id="PRO_0000018288"
SQ SEQUENCE 210 AA; 23633 MW; 5A350EB144248148 CRC64;
MLMFSRFRYI FFAVALLSGP VCAGARADLS AFTRGLKTLQ GHFSQEVIDT QGRVKERSNG
TVALSLPNLL RWECDAPYKQ LVVADGKRVW LFDPDLNQAS VLLQDNEERN SPLIALIDPI
QLDRKYDVSE EVAMRDGLRW LSLRPRGSTE ASFQSASFGF SQTQLARMEL VDNLGQRTVI
AFSGWQRNPV FAVNTFRFTP GKNVDVIGDR
