Q820B4 (LNT_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	lnt
Ordered Locus Names:	CBU_0564

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	485 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 – 485	485	Apolipoprotein N-acyltransferase HAMAP-Rule MF_01148		PRO_0000178061
Regions
	Transmembrane	15 – 37	23	Helical; Potential
	Transmembrane	44 – 66	23	Helical; Potential
	Transmembrane	76 – 98	23	Helical; Potential
	Transmembrane	111 – 133	23	Helical; Potential
	Transmembrane	157 – 179	23	Helical; Potential
	Transmembrane	186 – 208	23	Helical; Potential
	Transmembrane	467 – 484	18	Helical; Potential
	Domain	215 – 485	271	CN hydrolase

Sequences

	Sequence		Length	Mass (Da)
	Q820B4 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4F46FAB283EFA343	FASTA	485	54,620
	10 20 30 40 50 60 MNSVLALIAG AILPLAFAPF NWFPIAFVSP AILLAVWLRS RPLVAWWRGW LFGFGFFGAG 70 80 90 100 110 120 ASWVYVSIHH FGNANVPLAV LITVLFVFVL ALFIAFQGLS FSLFFRKRKA ALTALFAFPA 130 140 150 160 170 180 WWVVWEWLRS ILFTGFPWLF LGYSQINSPL KGFGPLFGIY GISLIVAFIS GCIYLLVTSK 190 200 210 220 230 240 KLNKKIMCLI LIILPFIVGW VLTFIPWTRP GSESVRVGLV QGNIGQRLKW DPDTLYSTLH 250 260 270 280 290 300 TYYSETQKNW DHGIIVWPEA AIPIYPQQVS VFLQALDKEA KQHNTALMTG IPIYHEKTNK 310 320 330 340 350 360 VFNGLMVLGD GHGLYLKRHL VPFGESFTSS KICNLLMKYF DIPMSDLSPG PEDQEPTVVK 370 380 390 400 410 420 GIPFAPFICY EIAYPTEVLN HLSNKQFIVV VNDDSWFAGT IAPAQQLQIA QMRALETERY 430 440 450 460 470 480 LLYSTNTGIT AIISPEGKIV KSAPQNQRLL LTGQIKPVTG KTPLMRWNYY PVVGIIIIFL LLTFL

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90108.1.
RefSeq	NP_819594.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q820B4.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_0564.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90108; AAO90108; CBU_0564.
GeneID	1208449.
KEGG	cbu:CBU_0564.
PATRIC	17929827. VBICoxBur82552_0558.
Phylogenomic databases
eggNOG	COG0815.
HOGENOM	HOG000264279.
KO	K03820.
OMA	HAFGWIT.
ProtClustDB	CLSK914152.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-568-MONOMER.
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_COXBU

Accession

Primary (citable) accession number: Q820B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program