ID   LPOB_KLEP7              Reviewed;         215 AA.
AC   A6T7G4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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};
GN   OrderedLocusNames=KPN78578_10740; ORFNames=KPN_01102;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR76535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6T7G4; -.
DR   SMR; A6T7G4; -.
DR   STRING; 272620.KPN_01102; -.
DR   jPOST; A6T7G4; -.
DR   DNASU; 5341235; -.
DR   EnsemblBacteria; ABR76535; ABR76535; KPN_01102.
DR   KEGG; kpn:KPN_01102; -.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   Proteomes; UP000000265; 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; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   CHAIN           20..215
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405785"
FT   REGION          28..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..58
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ   SEQUENCE   215 AA;  22554 MW;  BF71C8A17BC8AC29 CRC64;
     MMKMCRYALI TALAIFLAGC AGLREQPAPV EEAKPQPQQP AQPQPTVPTV PAVPSVPAQP
     GPIEHQDQQS GQPAPRVRHY DWNGAVQPLV GQMLQASGVN AGSILLVDSV NNRTNGSLNA
     GEATTALRSA LAGNGKFTLV SAQQLAVAKQ QLGLSPQDSL GSRSKAMGIA RNVGAQYVLY
     SNATGNVNAP ELKMQLMLVQ TGEIIWSGKG AVQQQ