ID   LOLB_ECOLI              Reviewed;         207 AA.
AC   P61320; P24208; Q46753;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   24-JAN-2024, entry version 160.
DE   RecName: Full=Outer-membrane lipoprotein LolB;
DE   Flags: Precursor;
GN   Name=lolB; Synonyms=hemM, ychC; OrderedLocusNames=b1209, JW1200;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1427085; DOI=10.1016/0378-1119(92)90170-t;
RA   Ikemi M., Murakami K., Hashimoto M., Murooka Y.;
RT   "Cloning and characterization of genes involved in the biosynthesis of
RT   delta-aminolevulinic acid in Escherichia coli.";
RL   Gene 121:127-132(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7679718; DOI=10.1099/00221287-139-2-259;
RA   Post D.A., Hove-Jensen B., Switzer R.L.;
RT   "Characterization of the hemA-prs region of the Escherichia coli and
RT   Salmonella typhimurium chromosomes: identification of two open reading
RT   frames and implications for prs expression.";
RL   J. Gen. Microbiol. 139:259-266(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7543480; DOI=10.1128/jb.177.15.4488-4500.1995;
RA   Strohmaier H., Remler P., Renner W., Hoegenauer G.;
RT   "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic
RT   acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is
RT   growth phase regulated primarily at the transcriptional level in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 177:4488-4500(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   CHARACTERIZATION, DIACYLGLYCEROL AT CYS-22, PALMITOYLATION AT CYS-22, AND
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=9384574; DOI=10.1093/emboj/16.23.6947;
RA   Matsuyama S., Yokota N., Tokuda H.;
RT   "A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA
RT   (p20)-dependent localization of lipoproteins to the outer membrane of
RT   Escherichia coli.";
RL   EMBO J. 16:6947-6955(1997).
RN   [8]
RP   IMPORTANCE FOR VIABILITY.
RC   STRAIN=K12;
RX   PubMed=11673422; DOI=10.1128/jb.183.22.6538-6542.2001;
RA   Tanaka K., Matsuyama S., Tokuda H.;
RT   "Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for
RT   Escherichia coli and causes accumulation of lipoprotein localization
RT   intermediates in the periplasm.";
RL   J. Bacteriol. 183:6538-6542(2001).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=12839983; DOI=10.1093/emboj/cdg324;
RA   Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.;
RT   "Crystal structures of bacterial lipoprotein localization factors, LolA and
RT   LolB.";
RL   EMBO J. 22:3199-3209(2003).
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       Essential for E.coli viability.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P61320; P61316: lolA; NbExp=2; IntAct=EBI-1122794, EBI-553532;
CC       P61320; P0A912: pal; NbExp=2; IntAct=EBI-1122794, EBI-1124760;
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC   -!- SIMILARITY: Belongs to the LolB family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be involved in delta-aminolevulinic
CC       acid biosynthesis. {ECO:0000305|PubMed:1427085}.
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DR   EMBL; M77237; AAA24433.1; -; Genomic_DNA.
DR   EMBL; D10264; BAA01105.1; -; Genomic_DNA.
DR   EMBL; U18555; AAC43435.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74293.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36067.1; -; Genomic_DNA.
DR   PIR; A47706; A47706.
DR   RefSeq; NP_415727.1; NC_000913.3.
DR   RefSeq; WP_001130692.1; NZ_SSZK01000010.1.
DR   PDB; 1IWM; X-ray; 1.90 A; A/B=22-207.
DR   PDB; 1IWN; X-ray; 2.20 A; A=22-207.
DR   PDBsum; 1IWM; -.
DR   PDBsum; 1IWN; -.
DR   AlphaFoldDB; P61320; -.
DR   SMR; P61320; -.
DR   BioGRID; 4260814; 301.
DR   DIP; DIP-35933N; -.
DR   IntAct; P61320; 9.
DR   MINT; P61320; -.
DR   STRING; 511145.b1209; -.
DR   DrugBank; DB02078; Triglyme.
DR   TCDB; 1.B.46.1.1; the outer membrane lolab lipoprotein insertion apparatus (lolab) family.
DR   jPOST; P61320; -.
DR   PaxDb; 511145-b1209; -.
DR   EnsemblBacteria; AAC74293; AAC74293; b1209.
DR   GeneID; 75203322; -.
DR   GeneID; 945775; -.
DR   KEGG; ecj:JW1200; -.
DR   KEGG; eco:b1209; -.
DR   PATRIC; fig|1411691.4.peg.1075; -.
DR   EchoBASE; EB1270; -.
DR   eggNOG; COG3017; Bacteria.
DR   HOGENOM; CLU_092816_1_1_6; -.
DR   InParanoid; P61320; -.
DR   OMA; FSSRFEW; -.
DR   OrthoDB; 9797618at2; -.
DR   PhylomeDB; P61320; -.
DR   BioCyc; EcoCyc:EG11293-MONOMER; -.
DR   BioCyc; MetaCyc:EG11293-MONOMER; -.
DR   EvolutionaryTrace; P61320; -.
DR   PRO; PR:P61320; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IDA:CACAO.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IMP:EcoCyc.
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   PANTHER; PTHR30634; OUTER MEMBRANE LOLAB LIPOPROTEIN INSERTION APPARATUS; 1.
DR   PANTHER; PTHR30634:SF13; OUTER-MEMBRANE LIPOPROTEIN LOLB-RELATED; 1.
DR   Pfam; PF03550; LolB; 1.
DR   SUPFAM; SSF89392; Prokaryotic lipoproteins and lipoprotein localization factors; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Chaperone; Direct protein sequencing;
KW   Lipoprotein; Membrane; Palmitate; Protein transport; Reference proteome;
KW   Signal; Transport.
FT   SIGNAL          1..21
FT   CHAIN           22..207
FT                   /note="Outer-membrane lipoprotein LolB"
FT                   /id="PRO_0000018296"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:9384574"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305|PubMed:9384574"
FT   CONFLICT        12
FT                   /note="L -> V (in Ref. 1; BAA01105)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41..42
FT                   /note="QH -> HD (in Ref. 3; AAC43435)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..207
FT                   /note="YDTKTQPAMPANMELTDGGQRIKLKMDNWIVK -> MTPKRNLRCQPIWNSP
FT                   TVVNASS (in Ref. 3; AAC43435)"
FT                   /evidence="ECO:0000305"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   HELIX           37..47
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          51..61
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          66..76
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          112..116
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   HELIX           132..138
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          157..166
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          168..173
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:1IWM"
FT   STRAND          196..207
FT                   /evidence="ECO:0007829|PDB:1IWM"
SQ   SEQUENCE   207 AA;  23551 MW;  C517F6E7353B8551 CRC64;
     MPLPDFRLIR LLPLAALVLT ACSVTTPKGP GKSPDSPQWR QHQQDVRNLN QYQTRGAFAY
     ISDQQKVYAR FFWQQTGQDR YRLLLTNPLG STELELNAQP GNVQLVDNKG QRYTADDAEE
     MIGKLTGMPI PLNSLRQWIL GLPGDATDYK LDDQYRLSEI TYSQNGKNWK VVYGGYDTKT
     QPAMPANMEL TDGGQRIKLK MDNWIVK
//