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 27-MAR-2024, entry version 64.
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; Pseudomonadota; 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 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 OrthoDB; 6466283at2; -.
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 Gene3D; 3.40.50.10610; ABC-type transport auxiliary lipoprotein component; 1.
DR HAMAP; MF_01889; LpoB; 1.
DR InterPro; IPR014094; LpoB.
DR NCBIfam; TIGR02722; lp; 1.
DR PANTHER; PTHR40593; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOB; 1.
DR PANTHER; PTHR40593:SF1; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOB; 1.
DR Pfam; PF13036; LpoB; 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
//
