(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ07_SHESH

ID   A8FQ07_SHESH            Unreviewed;       267 AA.
AC   A8FQ07;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Outer-membrane lipoprotein carrier protein {ECO:0000256|SAAS:SAAS01090847};
GN   OrderedLocusNames=Ssed_0317 {ECO:0000313|EMBL:ABV34930.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34930.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34930.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34930.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in the translocation of lipoproteins from
CC       the inner membrane to the outer membrane. Only forms a complex
CC       with a lipoprotein if the residue after the N-terminal Cys is not
CC       an aspartate (The Asp acts as a targeting signal to indicate that
CC       the lipoprotein should stay in the inner membrane).
CC       {ECO:0000256|SAAS:SAAS01090855}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS01090843}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|SAAS:SAAS01090846}.
CC   -!- SIMILARITY: Belongs to the LolA family.
CC       {ECO:0000256|SAAS:SAAS01090851}.
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DR   EMBL; CP000821; ABV34930.1; -; Genomic_DNA.
DR   RefSeq; WP_012004456.1; NC_009831.1.
DR   STRING; 425104.Ssed_0317; -.
DR   EnsemblBacteria; ABV34930; ABV34930; Ssed_0317.
DR   KEGG; sse:Ssed_0317; -.
DR   eggNOG; ENOG4108QTV; Bacteria.
DR   eggNOG; ENOG410ZJMM; LUCA.
DR   HOGENOM; HOG000286059; -.
DR   OMA; SVFHGDT; -.
DR   OrthoDB; 1933827at2; -.
DR   BioCyc; SSED425104:G1G9Y-333-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd16325; LolA; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
DR   SUPFAM; SSF89392; SSF89392; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ07.
DR   SWISS-2DPAGE; A8FQ07.
KW   Chaperone {ECO:0000256|SAAS:SAAS01090848};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Protein transport {ECO:0000256|SAAS:SAAS01090857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW   Transport {ECO:0000256|SAAS:SAAS01090850}.
SQ   SEQUENCE   267 AA;  29586 MW;  03C76E81EE9C0078 CRC64;
     MKTRERSYST WFATGLSRGK SVFGLLLLLS LSTFNVHATQ SSNYDTLFES SADNKRLQAL
     ADRLMIGESA SGSFTQYRTL KVLKKPLISH GHFIFDSRLG LVWQQTQPFE TTLILKEGEL
     IQIDSAGRRQ VSQAGSNQGA AAIAQTMPKL LSALLSGNLS DLSEHFNLYL KADDTRNEPQ
     EDEPAHWQLG LIPKDPLLVK AIPQMVLEGG EQVSALILLS NSGDSSRIEF EQISKAPLSQ
     EQRLFLSDRQ GEDSPKVQPE AKPEPYP
//

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