ID   LPOB_EDWTE              Reviewed;         197 AA.
AC   D0Z8F8;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=ETAE_1890;
OS   Edwardsiella tarda (strain EIB202).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=498217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EIB202;
RX   PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA   Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA   Zhao G., Liu Q., Zhang Y.;
RT   "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT   insights into its adaptation to broad host ranges and intracellular
RT   niches.";
RL   PLoS ONE 4:E7646-E7646(2009).
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; CP001135; ACY84727.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0Z8F8; -.
DR   SMR; D0Z8F8; -.
DR   EnsemblBacteria; ACY84727; ACY84727; ETAE_1890.
DR   KEGG; etr:ETAE_1890; -.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   Proteomes; UP000002634; 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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   CHAIN           18..197
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405782"
FT   REGION          23..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..56
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ   SEQUENCE   197 AA;  20329 MW;  C93D35EC42FB6D65 CRC64;
     MIKRMSGIAL AALLLSGCQG LLPRGETPSQ PPAPTTPAKP SVVPTPTPPV VTPVPQPPKM
     TSVDWQGSFA PLIDQLLSAP GVEAGSILLV DGVQNKTNGQ LSMANASEVL RSALAGNPRF
     QMVSTAQLAQ AKQSLGLAAN DSLGSRSKAI GLARQVSAQY VLYTTVSGNV QAPRLAMQLM
     LVQSGEIIWS GKGPVAL