P0AB38 (LPOB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Penicillin-binding protein activator LpoB
Short name=PBP activator LpoB

Alternative name(s):
Lipoprotein activator of PBP from the outer membrane B

Gene names

Name:	lpoB
Synonyms:	ycfM
Ordered Locus Names:	b1105, JW5157

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b. Ref.4 Ref.5
Subunit structure	Interacts with PBP1b. Ref.4 Ref.5
Subcellular location	Cell outer membrane; Lipid-anchor; Periplasmic side. Note: Localizes to the divisome and to the lateral wall. Ref.4 Ref.5
Disruption phenotype	Mutant shows sensitivity to many beta-lactams. Absence of both LpoA and LpoB leads to a decrease in peptide cross-linking and to cell lysis. Ref.4 Ref.5
Sequence similarities	Belongs to the LpoB family.

Ontologies

Keywords
Biological process	Cell shape Peptidoglycan synthesis
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
PTM	Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from direct assay Ref.4. Source: UniProtKB regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	internal side of cell outer membrane Inferred from direct assay Ref.4. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	enzyme regulator activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mrcB	P02919	4	EBI-3405489,EBI-909769

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 213	194	Penicillin-binding protein activator LpoB HAMAP-Rule MF_01889		PRO_0000168837
Amino acid modifications
	Lipidation	20	1	N-palmitoyl cysteine Potential
	Lipidation	20	1	S-diacylglycerol cysteine Potential

Sequences

	Sequence		Length	Mass (Da)
	P0AB38 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 06B529F3F4722AD7	FASTA	213	22,516
	10 20 30 40 50 60 MTKMSRYALI TALAMFLAGC VGQREPAPVE EVKPAPEQPA EPQQPVPTVP SVPTIPQQPG 70 80 90 100 110 120 PIEHEDQTAP PAPHIRHYDW NGAMQPMVSK MLGADGVTAG SVLLVDSVNN RTNGSLNAAE 130 140 150 160 170 180 ATETLRNALA NNGKFTLVSA QQLSMAKQQL GLSPQDSLGT RSKAIGIARN VGAHYVLYSS 190 200 210 ASGNVNAPTL QMQLMLVQTG EIIWSGKGAV SQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Regulation of peptidoglycan synthesis by outer-membrane proteins." Typas A., Banzhaf M., van den Berg van Saparoea B., Verheul J., Biboy J., Nichols R.J., Zietek M., Beilharz K., Kannenberg K., von Rechenberg M., Breukink E., den Blaauwen T., Gross C.A., Vollmer W. Cell 143:1097-1109(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PBP1B, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: K12.
[5]	"Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases." Paradis-Bleau C., Markovski M., Uehara T., Lupoli T.J., Walker S., Kahne D.E., Bernhardt T.G. Cell 143:1110-1120(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PBP1B, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74189.1. AP009048 Genomic DNA. Translation: BAA35912.2.
PIR	F64854.
RefSeq	NP_415623.1. NC_000913.2. YP_489373.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AB38.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AB38. 1 interaction.
STRING	511145.b1105.
Proteomic databases
PaxDb	P0AB38.
PRIDE	P0AB38.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74189; AAC74189; b1105. BAA35912; BAA35912; BAA35912.
GeneID	12934033. 948536.
KEGG	ecj:Y75_p1075. eco:b1105.
PATRIC	32117453. VBIEscCol129921_1149.
Organism-specific databases
EchoBASE	EB3205.
EcoGene	EG13431. lpoB.
Phylogenomic databases
eggNOG	COG3417.
HOGENOM	HOG000119084.
KO	K07337.
OMA	EIVWSGN.
ProtClustDB	CLSK879953.
Enzyme and pathway databases
BioCyc	EcoCyc:G6565-MONOMER. ECOL316407:JW5157-MONOMER.
Gene expression databases
Genevestigator	P0AB38.
Family and domain databases
HAMAP	MF_01889. LpoB.
InterPro	IPR014094. LpoB. [Graphical view]
Pfam	PF13036. DUF3897. 1 hit. [Graphical view]
TIGRFAMs	TIGR02722. lp_. 1 hit.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPOB_ECOLI

Accession

Primary (citable) accession number: P0AB38
Secondary accession number(s): P75947, Q9R424

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program