LOLB_CUPMC
ID LOLB_CUPMC Reviewed; 204 AA.
AC Q1LRP9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Rmet_0291;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07177.1; -; Genomic_DNA.
DR RefSeq; WP_011515179.1; NC_007973.1.
DR AlphaFoldDB; Q1LRP9; -.
DR SMR; Q1LRP9; -.
DR STRING; 266264.Rmet_0291; -.
DR EnsemblBacteria; ABF07177; ABF07177; Rmet_0291.
DR KEGG; rme:Rmet_0291; -.
DR eggNOG; COG3017; Bacteria.
DR HOGENOM; CLU_092816_3_0_4; -.
DR OMA; QIRQDGW; -.
DR OrthoDB; 1797257at2; -.
DR Proteomes; UP000002429; 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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT CHAIN 21..204
FT /note="Outer-membrane lipoprotein LolB"
FT /id="PRO_1000021675"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ SEQUENCE 204 AA; 22350 MW; 2E92BC027D2948F3 CRC64;
MLRSRRLALL CLATPLWLAA CASVTPTRGF DASETAASQL YTGRFSANYV RYGRNEGVQG
SFRWQEQGRN VRLDLVSPLG QTLAIVTATP SGATLDLPNE APRNAPEVDS LMEQALGFSL
PVSGMRDWLH GRAAPGTPSN VTRDANGRPD TLRQSGWTVR YLAWQDTPEN ATPTTTLPRR
IDMARDGNES PLSVRLVIDP ENKE