LOLB_ECOL6
ID LOLB_ECOL6 Reviewed; 207 AA.
AC Q8CW45;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 25-MAY-2022, entry version 98.
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}; Synonyms=hemM;
GN OrderedLocusNames=c1667;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN80132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN80132.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001130677.1; NC_004431.1.
DR AlphaFoldDB; Q8CW45; -.
DR SMR; Q8CW45; -.
DR STRING; 199310.c1667; -.
DR EnsemblBacteria; AAN80132; AAN80132; c1667.
DR KEGG; ecc:c1667; -.
DR eggNOG; COG3017; Bacteria.
DR HOGENOM; CLU_092816_1_1_6; -.
DR OMA; YQTRGSF; -.
DR Proteomes; UP000001410; 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; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT CHAIN 22..207
FT /note="Outer-membrane lipoprotein LolB"
FT /id="PRO_0000018297"
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 207 AA; 23615 MW; 83A448120ECB81DC CRC64;
MPLPDFRFIR LLPLAALVLT ACSITTPKGP GKSPDSPQWR QHQQDVRNLN QYQTRGAFAY
ISDQQKVYAR FFWQQTGQDR YRLLLTNPLG STELELNAQP GNVQLVDNKG QRYTSDDAEE
MIGKLTGMPI PLNSLRQWIL GLPGDATDYK LDDQYRLSEI TYSQNGKNWK VVYGGYDTKT
QPAMPANMEL TDGGQRIKLK MDNWIVK