ID LPOB_CROTZ Reviewed; 221 AA.
AC C9Y1J4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 24-JAN-2024, entry version 66.
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=Ctu_16840;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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 -!- SEQUENCE CAUTION:
CC Sequence=CBA29978.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN543093; CBA29978.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C9Y1J4; -.
DR SMR; C9Y1J4; -.
DR KEGG; ctu:CTU_16840; -.
DR PATRIC; fig|693216.3.peg.1607; -.
DR HOGENOM; CLU_092328_0_0_6; -.
DR Proteomes; UP000002069; 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 Gene3D; 3.40.50.10610; ABC-type transport auxiliary lipoprotein component; 1.
DR HAMAP; MF_01889; LpoB; 1.
DR InterPro; IPR014094; LpoB.
DR NCBIfam; TIGR02722; lp; 1.
DR PANTHER; PTHR40593; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOB; 1.
DR PANTHER; PTHR40593:SF1; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOB; 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; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT CHAIN 21..221
FT /note="Penicillin-binding protein activator LpoB"
FT /id="PRO_0000405780"
FT REGION 29..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ SEQUENCE 221 AA; 23184 MW; 8BD9A7BAB470BAB7 CRC64;
MLNRMYRYAL LATVALALSG CILPGEQKPA PVEEAQPGTQ QPTQPVPPPT QPVPTVPSVP
SIPAQPGPIE HQPENATPEP KARTYDWNSA MAPMVGKMLQ ADGVNAGSVL LVDSVNNRTN
GSLQTGPATE ALRGALANNA KFTLVSAQQL SMAKQQLGLS PQDSLGSRSK AIGIARNVGA
QYVLYANASG NVNAPTLQMQ LMLVQTGEII WSGKGAVQQT Q
//
