LOLA_SHESM
ID LOLA_SHESM Reviewed; 206 AA.
AC Q0HIT0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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};
GN OrderedLocusNames=Shewmr4_1964;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000446; ABI39037.1; -; Genomic_DNA.
DR RefSeq; WP_011622730.1; NC_008321.1.
DR AlphaFoldDB; Q0HIT0; -.
DR SMR; Q0HIT0; -.
DR KEGG; she:Shewmr4_1964; -.
DR HOGENOM; CLU_087560_1_1_6; -.
DR OMA; YDPFVEQ; -.
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..206
FT /note="Outer-membrane lipoprotein carrier protein"
FT /id="PRO_5000129834"
SQ SEQUENCE 206 AA; 22953 MW; 20D2DB0258B31293 CRC64;
MKKLLCAVLL SPLLYSNAVL ADDAKQLRET LNGTESLKAD FKQTVTDINK KVIQTGAGVF
ALAHPNQFYW HLTAPDESQI VADGKDLWIY NPFAEEVVIM DFAEAINASP IALLVHRDDA
TWSQYSVTKK QDCYEIKPKS TDAGITSVNV CFNKGTLNKF NVLDDKGNLS QFDLSNQHSI
NAADKALFKF VLPENVDVDD QRLKTQ