ID LOLB_BORPD Reviewed; 199 AA.
AC A9I6X6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Bpet4004;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP44352.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I6X6; -.
DR SMR; A9I6X6; -.
DR STRING; 94624.Bpet4004; -.
DR KEGG; bpt:Bpet4004; -.
DR eggNOG; COG3017; Bacteria.
DR Proteomes; UP000001225; 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 Gene3D; 2.50.20.10; Lipoprotein localisation LolA/LolB/LppX; 1.
DR HAMAP; MF_00233; LolB; 1.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR004565; OM_lipoprot_LolB.
DR NCBIfam; TIGR00548; lolB; 1.
DR Pfam; PF03550; LolB; 1.
DR SUPFAM; SSF89392; Prokaryotic lipoproteins and lipoprotein localization factors; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Protein transport; Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT CHAIN 29..199
FT /note="Outer-membrane lipoprotein LolB"
FT /id="PRO_1000100490"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ SEQUENCE 199 AA; 21026 MW; 8A4F0210D911CABB CRC64;
MAAAGSLCQT AWRVRGWLAA GLCALLAGCA SVPDAPSGTA EGAFSRGGRF AITMTESSGE
QQAVQGGFTW RDDGRRYQLD LTNPLGSTEA RVEGRPGHAT LTKADGTVLQ ADTPDALVEE
ALGSPVPVSG LRDWLRGRVA DDAPAGKLQS DAQGRPLSFE QDGWQARLSR YDDQGPGLLV
LQRTEPGRRI VVRLAVSQP
//
