ID   LPOB_ERWAC              Reviewed;         198 AA.
AC   D4I110;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Penicillin-binding protein activator LpoB {ECO:0000255|HAMAP-Rule:MF_01889};
DE            Short=PBP activator LpoB {ECO:0000255|HAMAP-Rule:MF_01889};
DE   Flags: Precursor;
GN   Name=lpoB {ECO:0000255|HAMAP-Rule:MF_01889}; OrderedLocusNames=EAMY_1485;
OS   Erwinia amylovora (strain CFBP1430).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=665029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP1430;
RX   PubMed=20192826; DOI=10.1094/mpmi-23-4-0384;
RA   Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT   CFBP 1430 and comparison to other Erwinia spp.";
RL   Mol. Plant Microbe Interact. 23:384-393(2010).
CC   -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC       the function of penicillin-binding protein 1B (PBP1b).
CC       {ECO:0000255|HAMAP-Rule:MF_01889}.
CC   -!- SUBUNIT: Interacts with PBP1b. {ECO:0000255|HAMAP-Rule:MF_01889}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01889}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01889};
CC       Periplasmic side {ECO:0000255|HAMAP-Rule:MF_01889}.
CC   -!- SIMILARITY: Belongs to the LpoB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01889}.
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DR   EMBL; FN434113; CBA20435.1; -; Genomic_DNA.
DR   RefSeq; WP_004157139.1; NC_013961.1.
DR   AlphaFoldDB; D4I110; -.
DR   SMR; D4I110; -.
DR   STRING; 665029.EAMY_1485; -.
DR   EnsemblBacteria; CBA20435; CBA20435; EAMY_1485.
DR   GeneID; 8914395; -.
DR   KEGG; eam:EAMY_1485; -.
DR   PATRIC; fig|665029.3.peg.1445; -.
DR   eggNOG; COG3417; Bacteria.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   OrthoDB; 1716742at2; -.
DR   Proteomes; UP000001841; Chromosome.
DR   GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_01889; LpoB; 1.
DR   InterPro; IPR014094; LpoB.
DR   PANTHER; PTHR40593; PTHR40593; 1.
DR   Pfam; PF13036; LpoB; 1.
DR   TIGRFAMs; TIGR02722; lp; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW   Peptidoglycan synthesis; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   CHAIN           21..198
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405783"
FT   REGION          28..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..62
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ   SEQUENCE   198 AA;  20829 MW;  98A3036D89E745D7 CRC64;
     MSWIRIRRSG VLLLALVLSG CINQQQQPQP AAPVEPVTPP VNVPQPPKAE PGQNVPPPPK
     MQPLNWSATV SPLVGQMLKA DGINAGNVLL VDNVKNSTNG SLQSAKATAA LLNSLENNGQ
     FSLVTPQQLA AARQTLGLSA DDSLVSRSKA IGLARYVGAQ YVLYSNAEGD IKSPSLQLQL
     MLVQTGEIIW SGSGAVVH