ID   LPOB_ENT38              Reviewed;         216 AA.
AC   A4W9B9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Ent638_1620;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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; CP000653; ABP60299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4W9B9; -.
DR   SMR; A4W9B9; -.
DR   STRING; 399742.Ent638_1620; -.
DR   EnsemblBacteria; ABP60299; ABP60299; Ent638_1620.
DR   KEGG; ent:Ent638_1620; -.
DR   eggNOG; COG3417; Bacteria.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   OrthoDB; 1716742at2; -.
DR   Proteomes; UP000000230; 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..216
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_5000237839"
FT   REGION          28..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..63
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   216 AA;  22840 MW;  30A433FEDE81C1E4 CRC64;
     MIKNLSRYAL VTAFALFLSG CITRTEQQPA PVDEAKPGTE QPAQPTQPVP TVPSVPTVPA
     QPGPIEHPDQ TSQPAPRVRH YDWNGAMQPM VGKMLQAQGV TAGSVLLVDS VNNRTNGTLN
     AGEATETLRN ALANNGKFTL VSAQQLAVAK QQLGLSPQDS LGSRSKAMGI ARNVGAQYVL
     YSNATGNVNT PALQMQLMLV QTGEIIWSGK GAVSQQ