ID   LPOB_SHISS              Reviewed;         213 AA.
AC   Q3Z312;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=SSON_1125;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87850.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z312; -.
DR   BMRB; Q3Z312; -.
DR   SMR; Q3Z312; -.
DR   EnsemblBacteria; AAZ87850; AAZ87850; SSON_1125.
DR   KEGG; ssn:SSON_1125; -.
DR   HOGENOM; CLU_092328_0_0_6; -.
DR   OMA; AMQPMVG; -.
DR   Proteomes; UP000002529; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT   CHAIN           20..213
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405791"
FT   REGION          28..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..57
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   213 AA;  22516 MW;  06B529F3F4722AD7 CRC64;
     MTKMSRYALI TALAMFLAGC VGQREPAPVE EVKPAPEQPA EPQQPVPTVP SVPTIPQQPG
     PIEHEDQTAP PAPHIRHYDW NGAMQPMVSK MLGADGVTAG SVLLVDSVNN RTNGSLNAAE
     ATETLRNALA NNGKFTLVSA QQLSMAKQQL GLSPQDSLGT RSKAIGIARN VGAHYVLYSS
     ASGNVNAPTL QMQLMLVQTG EIIWSGKGAV SQQ