P44626 (LNT_HAEIN) 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 homolog

Gene names

Name:	lnt
Synonyms:	cutE
Ordered Locus Names:	HI_0302

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Transfers the fatty acyl group on membrane lipoproteins By similarity. HAMAP-Rule MF_01148
Pathway	Protein modification; lipoprotein biosynthesis (N-acyl transfer). HAMAP-Rule MF_01148
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01148.
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
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipoprotein biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP 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 – 522	522	Apolipoprotein N-acyltransferase HAMAP-Rule MF_01148		PRO_0000178068
Regions
	Transmembrane	17 – 37	21	Helical; Potential
	Transmembrane	61 – 81	21	Helical; Potential
	Transmembrane	98 – 118	21	Helical; Potential
	Transmembrane	164 – 184	21	Helical; Potential
	Transmembrane	197 – 217	21	Helical; Potential
	Transmembrane	495 – 515	21	Helical; Potential
	Domain	231 – 517	287	CN hydrolase

Sequences

	Sequence		Length	Mass (Da)
	P44626 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 8D327E5C50053C8F	FASTA	522	58,553
	10 20 30 40 50 60 MKNLNRILLS IKFMNKYFTY LIAIISGLLG VFAFSPFDYW PLAYVSLLGL LYVAKNPKKS 70 80 90 100 110 120 TALLSTFLWA MGFFCFGVSW LNVSIHQFGG ASLGVSYFLV GLLAAYLALY PMLFTYLVHH 130 140 150 160 170 180 FKVQSAVIFA VIWTLTEFLR GWIFTGFPWL QFGYTQIDSP FYGIAPIFGV TGLTFFTVWA 190 200 210 220 230 240 SAVIFNLVSS LFKTKNLKLV LANALLLIIV GGLSAYSSRI HFVKSVEDKA ISVTLAQGNI 250 260 270 280 290 300 EQNLKWDPNY FYSTLAIYQK LITENLGKTD LIILPESALP TLENAITPFF EGLERAAKET 310 320 330 340 350 360 KTEIMVGTVF QDTKSGKLLN SIMTAGNPDF PYQPNTQNRY NKHHLVPFGE YVPLESILRP 370 380 390 400 410 420 LNSVFNLPMS AFQSGEAVQP SLIAKKRAFS PAICYEIIFG EQVRQNLKQD TDYLLTLSND 430 440 450 460 470 480 AWFGDSIGPW QHLQMARMRA LELGKPLIRA TNTGISVFVD AQGKVLAQAP QFIETTLTYK 490 500 510 520 IAPAEGKTPY SVLGNMPLYA LSLLFLLLHS MMAFIRRKMN IL

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21967.1.
PIR	H64060.
RefSeq	NP_438469.2. NC_000907.1.
3D structure databases
ProteinModelPortal	P44626.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0302.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC21967; AAC21967; HI_0302.
GeneID	949425.
KEGG	hin:HI0302.
PATRIC	20189145. VBIHaeInf48452_0319.
Phylogenomic databases
eggNOG	COG0815.
KO	K03820.
OMA	HAWTHSA.
ProtClustDB	PRK00302.
Enzyme and pathway databases
UniPathway	UPA00666.
Family and domain databases
Gene3D	3.60.110.10. 1 hit.
HAMAP	MF_01148. Lnt.
InterPro	IPR004563. Apolipo_AcylTrfase. IPR003010. C-N_Hydrolase. [Graphical view]
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_HAEIN

Accession

Primary (citable) accession number: P44626

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program