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   25-MAY-2022, entry version 71.
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; Proteobacteria; 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   EnsemblBacteria; CAP44352; CAP44352; Bpet4004.
DR   KEGG; bpt:Bpet4004; -.
DR   eggNOG; COG3017; Bacteria.
DR   OMA; QIRQDGW; -.
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   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.
PE   3: Inferred from homology;
KW   Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW   Protein transport; Reference proteome; 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