P23930 (LNT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein N-acyltransferase
Short name=ALP N-acyltransferase
EC=2.3.1.-

Alternative name(s):
Copper homeostasis protein CutE

Gene names

Name:	lnt
Synonyms:	cutE
Ordered Locus Names:	b0657, JW0654

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfers the fatty acyl group on membrane lipoproteins. HAMAP MF_01148
Pathway	Protein modification; lipoprotein biosynthesis (N-acyl transfer). HAMAP MF_01148
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.6 Ref.8.
Sequence similarities	Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily. Contains 1 CN hydrolase domain.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipoprotein biosynthetic process Inferred from electronic annotation. Source: InterPro nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acyltransferase activity Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 512	512	Apolipoprotein N-acyltransferase HAMAP MF_01148		PRO_0000178062
Regions
	Transmembrane	12 – 28	17	Helical; Potential
	Transmembrane	57 – 77	21	Helical; Potential
	Transmembrane	91 – 111	21	Helical; Potential
	Transmembrane	168 – 188	21	Helical; Potential
	Transmembrane	194 – 214	21	Helical; Potential
	Transmembrane	487 – 507	21	Helical; Potential
	Domain	222 – 512	291	CN hydrolase
	Region	425 – 431	7	Could contain a copper-binding motif HAMAP MF_01148
Experimental info
	Sequence conflict	186	1	A → V Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23930 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 70CFD6627C286615	FASTA	512	57,066
	10 20 30 40 50 60 MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG 70 80 90 100 110 120 FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT 130 140 150 160 170 180 WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPIMGVE AINFLLMMVS 190 200 210 220 230 240 GLLALALVKR NWRPLVVAVV LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG 250 260 270 280 290 300 QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV 310 320 330 340 350 360 DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL 370 380 390 400 410 420 PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILGEQVRDNF RPDTDYLLTI SNDAWFGKSI 430 440 450 460 470 480 GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFTREVL TTNVTPTTGL 490 500 510 TPYARTGNWP LWVLTALFGF AAVLMSLRQR RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of cutE, a gene involved in copper transport in Escherichia coli." Rogers S.D., Bhave M.R., Mercer J.F.B., Camakaris J., Lee B.T.O. J. Bacteriol. 173:6742-6748(1991) [PubMed: 1938881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 186. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli." Gupta S.D., Wu H.C. FEMS Microbiol. Lett. 62:37-41(1991) [PubMed: 2032623] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase." Gupta S.D., Gan K., Schmid M.B., Wu H.C. J. Biol. Chem. 268:16551-16556(1993) [PubMed: 8344936] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58070 Genomic DNA. Translation: CAA41100.1. U82598 Genomic DNA. Translation: AAB40859.1. U00096 Genomic DNA. Translation: AAC73758.1. AP009048 Genomic DNA. Translation: BAA35308.2.
PIR	S18194.
RefSeq	NP_415190.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P23930.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10111N.
IntAct	P23930. 1 interaction.
MINT	MINT-1238661.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003488; EBESCP00000003488; EBESCG00000002863. EBESCT00000014779; EBESCP00000014070; EBESCG00000013839.
GeneID	946201.
GenomeReviews	Gene locus JW0654 in contig AP009048_GR. Gene locus b0657 in contig U00096_GR.
KEGG	ecj:JW0654. eco:b0657.
PATRIC	32116503. VBIEscCol129921_0691.
Organism-specific databases
EchoBASE	EB0166.
EcoGene	EG10168. cutE.
Phylogenomic databases
eggNOG	COG0815.
GeneTree	EBGT00050000010323.
HOGENOM	HBG616234.
OMA	IAPYICY.
PhylomeDB	P23930.
ProtClustDB	PRK00302.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10168-MONOMER.
Gene expression databases
Genevestigator	P23930.
Family and domain databases
HAMAP	MF_01148. Lnt. [Tree]
InterPro	IPR004563. Apolipo_AcylTrfase. IPR003010. Ntlse/CNhydtse. [Graphical view]
Gene3D	G3DSA:3.60.110.10. Ntlse/CNhydtse. 1 hit.
KO	K03820.
Pfam	PF00795. CN_hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56317. Ntlse/CNhydtse. 1 hit.
TIGRFAMs	TIGR00546. Lnt. 1 hit.
PROSITE	PS50263. CN_HYDROLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LNT_ECOLI

Accession

Primary (citable) accession number: P23930
Secondary accession number(s): P77703

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program