LPOB_PHOLL
ID LPOB_PHOLL Reviewed; 189 AA.
AC Q7N395;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=plu2824;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571868; CAE15198.1; -; Genomic_DNA.
DR RefSeq; WP_011147044.1; NC_005126.1.
DR AlphaFoldDB; Q7N395; -.
DR SMR; Q7N395; -.
DR STRING; 243265.plu2824; -.
DR EnsemblBacteria; CAE15198; CAE15198; plu2824.
DR GeneID; 24170366; -.
DR KEGG; plu:plu2824; -.
DR eggNOG; COG3417; Bacteria.
DR HOGENOM; CLU_092328_0_0_6; -.
DR OMA; AMQPMVG; -.
DR OrthoDB; 1716742at2; -.
DR BioCyc; PLUM243265:PLU_RS14010-MON; -.
DR Proteomes; UP000002514; 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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT CHAIN 17..189
FT /note="Penicillin-binding protein activator LpoB"
FT /id="PRO_0000405788"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..49
FT /note="Pro residues"
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 189 AA; 20675 MW; 24D88A11632E335E CRC64;
MRRILFVALS VMFLAGCPSL PPEQPEPPTP VVPVTPSEKP TPPSEKVPEP PKMSAIDWES
TVQPLVEQLV KAHGLENAKL LLVDTVKNNT NGALQTMQAT DALRQAISSE HVFELIPQNQ
VQNARQSLGL SEEDSLGLRS KAIGLARYLN AEYVLYSIVS GNSDKRDIVM QLMLVKTGEI
LWSGHGDVK