LOLB_SHEFN
ID LOLB_SHEFN Reviewed; 203 AA.
AC Q087I6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Outer-membrane lipoprotein LolB {ECO:0000255|HAMAP-Rule:MF_00233};
DE Flags: Precursor;
GN Name=lolB {ECO:0000255|HAMAP-Rule:MF_00233}; OrderedLocusNames=Sfri_0721;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a critical role in the incorporation of lipoproteins in
CC the outer membrane after they are released by the LolA protein.
CC {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00233}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SIMILARITY: Belongs to the LolB family. {ECO:0000255|HAMAP-
CC Rule:MF_00233}.
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DR EMBL; CP000447; ABI70579.1; -; Genomic_DNA.
DR AlphaFoldDB; Q087I6; -.
DR SMR; Q087I6; -.
DR STRING; 318167.Sfri_0721; -.
DR EnsemblBacteria; ABI70579; ABI70579; Sfri_0721.
DR KEGG; sfr:Sfri_0721; -.
DR eggNOG; COG3017; Bacteria.
DR HOGENOM; CLU_092816_1_0_6; -.
DR OMA; YQTRGSF; -.
DR Proteomes; UP000000684; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd16326; LolB; 1.
DR HAMAP; MF_00233; LolB; 1.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR004565; OM_lipoprot_LolB.
DR Pfam; PF03550; LolB; 1.
DR SUPFAM; SSF89392; SSF89392; 1.
DR TIGRFAMs; TIGR00548; lolB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT CHAIN 22..203
FT /note="Outer-membrane lipoprotein LolB"
FT /id="PRO_0000336618"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ SEQUENCE 203 AA; 22318 MW; 9CA85D962E3BB13C CRC64;
MRLSASLFHI ALVTVLLVLA GCSVTPSEDF SPINVTNAAQ AKAWELQGKI AVKTSEDKFS
TNLYWLHQTK ANDLRLTTVL GTTVLTLKTN QGMATLDVDG KTYRDSNAQD LLTGISGWSI
PLDSLPLWIT GQIGSNDKIV SYNPDGTIKQ LISHDPEANW VVSFLGWQQQ SGAQVPRLLK
IEREDVQIKI QTNQWIAVAA KTK