LOLA_KLEP3
ID LOLA_KLEP3 Reviewed; 203 AA.
AC B5XYA1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=KPK_3637;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08657.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XYA1; -.
DR SMR; B5XYA1; -.
DR PRIDE; B5XYA1; -.
DR EnsemblBacteria; ACI08657; ACI08657; KPK_3637.
DR KEGG; kpe:KPK_3637; -.
DR HOGENOM; CLU_087560_1_1_6; -.
DR OMA; YDPFVEQ; -.
DR OrthoDB; 1933827at2; -.
DR Proteomes; UP000001734; 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..203
FT /note="Outer-membrane lipoprotein carrier protein"
FT /id="PRO_1000100721"
FT REGION 184..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22574 MW; FC3C04136C60866E CRC64;
MKKLAITCAL LSGMVVSQVW ADAASDLKSR LDKVSSFHAS FTQKVTDGSG NAVQDGQGDL
WVKRPNLFNW HMTQPDESVL VSDGKTLWFY NPFVEQATAT WLKDATSNTP FMLIARNQSS
DWQQYNIKQN GDDFVLTPKS GSGNLKQFTI NVGRDGTIHQ FSAVEQDDQR SSYQLKSQQN
GAVDASKFTF TPPKGVTVDD QRK