LPOB_ECOLI
ID LPOB_ECOLI Reviewed; 213 AA.
AC P0AB38; P75947; Q9R424;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Penicillin-binding protein activator LpoB;
DE Short=PBP activator LpoB;
DE AltName: Full=Lipoprotein activator of PBP from the outer membrane B;
DE Flags: Precursor;
GN Name=lpoB; Synonyms=ycfM; OrderedLocusNames=b1105, JW5157;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, INTERACTION WITH PBP1B, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=21183073; DOI=10.1016/j.cell.2010.11.038;
RA Typas A., Banzhaf M., van den Berg van Saparoea B., Verheul J., Biboy J.,
RA Nichols R.J., Zietek M., Beilharz K., Kannenberg K., von Rechenberg M.,
RA Breukink E., den Blaauwen T., Gross C.A., Vollmer W.;
RT "Regulation of peptidoglycan synthesis by outer-membrane proteins.";
RL Cell 143:1097-1109(2010).
RN [5]
RP FUNCTION, INTERACTION WITH PBP1B, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21183074; DOI=10.1016/j.cell.2010.11.037;
RA Paradis-Bleau C., Markovski M., Uehara T., Lupoli T.J., Walker S.,
RA Kahne D.E., Bernhardt T.G.;
RT "Lipoprotein cofactors located in the outer membrane activate bacterial
RT cell wall polymerases.";
RL Cell 143:1110-1120(2010).
CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC the function of penicillin-binding protein 1B (PBP1b). Stimulates
CC transpeptidase and transglycosylase activities of PBP1b in vitro. May
CC also contribute to outer membrane constriction during cell division, in
CC complex with PBP1b. {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}.
CC -!- SUBUNIT: Interacts with PBP1b. {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}.
CC -!- INTERACTION:
CC P0AB38; P02919: mrcB; NbExp=4; IntAct=EBI-3405489, EBI-909769;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}; Lipid-anchor
CC {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Periplasmic
CC side {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}.
CC Note=Localizes to the divisome and to the lateral wall.
CC -!- DISRUPTION PHENOTYPE: Mutant shows sensitivity to many beta-lactams.
CC Absence of both LpoA and LpoB leads to a decrease in peptide cross-
CC linking and to cell lysis. {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}.
CC -!- SIMILARITY: Belongs to the LpoB family. {ECO:0000305}.
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DR EMBL; U00096; AAC74189.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35912.2; -; Genomic_DNA.
DR PIR; F64854; F64854.
DR RefSeq; NP_415623.1; NC_000913.3.
DR RefSeq; WP_000164439.1; NZ_STEB01000016.1.
DR AlphaFoldDB; P0AB38; -.
DR BMRB; P0AB38; -.
DR SMR; P0AB38; -.
DR BioGRID; 4263027; 152.
DR BioGRID; 852830; 8.
DR IntAct; P0AB38; 10.
DR STRING; 511145.b1105; -.
DR jPOST; P0AB38; -.
DR PaxDb; P0AB38; -.
DR PRIDE; P0AB38; -.
DR EnsemblBacteria; AAC74189; AAC74189; b1105.
DR EnsemblBacteria; BAA35912; BAA35912; BAA35912.
DR GeneID; 66670629; -.
DR GeneID; 948536; -.
DR KEGG; ecj:JW5157; -.
DR KEGG; eco:b1105; -.
DR PATRIC; fig|1411691.4.peg.1162; -.
DR EchoBASE; EB3205; -.
DR eggNOG; COG3417; Bacteria.
DR HOGENOM; CLU_092328_0_0_6; -.
DR OMA; AMQPMVG; -.
DR PhylomeDB; P0AB38; -.
DR BioCyc; EcoCyc:G6565-MON; -.
DR BioCyc; MetaCyc:G6565-MON; -.
DR PRO; PR:P0AB38; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:UniProtKB.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW Peptidoglycan synthesis; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..213
FT /note="Penicillin-binding protein activator LpoB"
FT /id="PRO_0000168837"
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"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
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
