LPOB_PANAM
ID LPOB_PANAM Reviewed; 198 AA.
AC D4GC59;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=PANA_1495;
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103;
RX PubMed=20348253; DOI=10.1128/jb.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001875; ADD76662.1; -; Genomic_DNA.
DR RefSeq; WP_013025378.1; NC_013956.2.
DR AlphaFoldDB; D4GC59; -.
DR SMR; D4GC59; -.
DR STRING; 706191.PANA_1495; -.
DR EnsemblBacteria; ADD76662; ADD76662; PANA_1495.
DR GeneID; 57268698; -.
DR KEGG; pam:PANA_1495; -.
DR eggNOG; COG3417; Bacteria.
DR HOGENOM; CLU_092328_0_0_6; -.
DR OMA; AMQPMVG; -.
DR OrthoDB; 1716742at2; -.
DR BioCyc; PANA706191:PANA_RS07645-MON; -.
DR Proteomes; UP000001702; 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..198
FT /note="Penicillin-binding protein activator LpoB"
FT /id="PRO_0000405786"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..59
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 198 AA; 21123 MW; 4B91F8ED5E6CCDA9 CRC64;
MIRSVNRTGA LMMALILSGC VMKQQQPAPV EPTQPVEPVQ PVPQPEQPIP QPQPVPQPPK
LVTINWDASV EPLVAQMVRA ATVTPGSVLL VDRIKNSTNG ALQGEKATSA IQNALNNNGK
FTLVSSEQLA QAKQTLGLSP DDSLNSRSKA IGLARNLNAQ YVLYSTAKGD VKSPTLQMQL
MLVQTGEIIW SGNGVAQN
