ID   LPOB_HAMD5              Reviewed;         198 AA.
AC   C4K8P0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Penicillin-binding protein activator LpoB;
DE            Short=PBP activator LpoB;
DE   Flags: Precursor;
GN   Name=lpoB; OrderedLocusNames=HDEF_0102;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
CC   -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC       the function of penicillin-binding protein 1B (PBP1b). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PBP1b. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LpoB family. {ECO:0000305}.
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DR   EMBL; CP001277; ACQ66877.1; -; Genomic_DNA.
DR   RefSeq; WP_012737842.1; NC_012751.1.
DR   AlphaFoldDB; C4K8P0; -.
DR   SMR; C4K8P0; -.
DR   STRING; 572265.HDEF_0102; -.
DR   EnsemblBacteria; ACQ66877; ACQ66877; HDEF_0102.
DR   GeneID; 66260041; -.
DR   KEGG; hde:HDEF_0102; -.
DR   eggNOG; COG3417; Bacteria.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   Proteomes; UP000002334; 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   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; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           17..198
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405784"
FT   REGION          23..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   198 AA;  21397 MW;  82C47D0A62475292 CRC64;
     MKKYLLSASI VFLLASCAQP PAKIGRPSKS EPSTVSTDSP EGISSESAEI GIVPLTPKIK
     SFDWSVPMKP LVENMSQTKD LPNGSVLLVD TVKNNTNGLL QIEKATESLL HILSSNNTFF
     LISANQLAKA KTALGISKQD NLSSRSKAIA LGRYLKAEYV LYTDVSDDIQ SPVINMELML
     VKTGEIIWAD KTAMTLAP