ID   LPOB_PROMH              Reviewed;         193 AA.
AC   B4EVE5;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=PMI0871;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR41968.1; -; Genomic_DNA.
DR   RefSeq; WP_004247096.1; NC_010554.1.
DR   AlphaFoldDB; B4EVE5; -.
DR   SMR; B4EVE5; -.
DR   STRING; 529507.PMI0871; -.
DR   EnsemblBacteria; CAR41968; CAR41968; PMI0871.
DR   GeneID; 6803410; -.
DR   KEGG; pmr:PMI0871; -.
DR   eggNOG; COG3417; Bacteria.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   Proteomes; UP000008319; 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   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|HAMAP-Rule:MF_01889"
FT   CHAIN           17..193
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405789"
FT   REGION          23..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ   SEQUENCE   193 AA;  20645 MW;  51E4C127A96E87FA CRC64;
     MKKMLFVVAA VFLLAGCPSM LPQQPPAPVE PVTPTEPTEP PKPIEPPIEV VPTPPKITSI
     NWNAAIQPLI REMSVTDDLA TGKLLVVDNV KNNSGGNIQA VNATNTIIDS VNSISALQTV
     PYAQMMSARK ALGLSGEDSL GLRSAAIGLA RYLQADYILF STVDGKKDNR VISMQLMSVA
     SGEILWSGRH KVE