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Protein

Apolipoprotein N-acyltransferase

Gene

lnt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transfers the fatty acyl group on membrane lipoproteins.

Pathwayi: lipoprotein biosynthesis (N-acyl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (N-acyl transfer) and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei267Proton acceptorPROSITE-ProRule annotation1
Active sitei335PROSITE-ProRule annotation1
Active sitei387NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

  • N-acyltransferase activity Source: EcoCyc

GO - Biological processi

  • lipoprotein biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionAcyltransferase, Transferase
LigandCopper

Enzyme and pathway databases

BioCyciEcoCyc:EG10168-MONOMER
MetaCyc:EG10168-MONOMER
UniPathwayiUPA00666

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein N-acyltransferase (EC:2.3.1.-)
Short name:
ALP N-acyltransferase
Alternative name(s):
Copper homeostasis protein CutE
Gene namesi
Name:lnt
Synonyms:cutE
Ordered Locus Names:b0657, JW0654
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10168 cutE

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei12 – 28HelicalSequence analysisAdd BLAST17
Transmembranei57 – 77HelicalSequence analysisAdd BLAST21
Transmembranei91 – 111HelicalSequence analysisAdd BLAST21
Transmembranei168 – 188HelicalSequence analysisAdd BLAST21
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Transmembranei487 – 507HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001780621 – 512Apolipoprotein N-acyltransferaseAdd BLAST512

Proteomic databases

PaxDbiP23930
PRIDEiP23930

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
pykAP215993EBI-556569,EBI-368956

Protein-protein interaction databases

BioGridi4259916, 206 interactors
DIPiDIP-10111N
IntActiP23930, 2 interactors
STRINGi316385.ECDH10B_0726

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi10 – 23Combined sources14
Helixi24 – 27Combined sources4
Turni29 – 31Combined sources3
Helixi35 – 47Combined sources13
Turni48 – 50Combined sources3
Helixi53 – 71Combined sources19
Helixi75 – 83Combined sources9
Helixi87 – 115Combined sources29
Helixi121 – 125Combined sources5
Helixi127 – 139Combined sources13
Helixi142 – 144Combined sources3
Helixi153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Helixi161 – 163Combined sources3
Helixi164 – 167Combined sources4
Helixi169 – 189Combined sources21
Helixi192 – 203Combined sources12
Helixi206 – 210Combined sources5
Beta strandi214 – 216Combined sources3
Helixi218 – 220Combined sources3
Beta strandi222 – 228Combined sources7
Helixi233 – 236Combined sources4
Helixi239 – 241Combined sources3
Helixi242 – 253Combined sources12
Helixi254 – 256Combined sources3
Turni257 – 259Combined sources3
Beta strandi261 – 264Combined sources4
Beta strandi270 – 273Combined sources4
Helixi274 – 277Combined sources4
Helixi278 – 290Combined sources13
Beta strandi294 – 304Combined sources11
Beta strandi310 – 320Combined sources11
Beta strandi332 – 334Combined sources3
Turni341 – 343Combined sources3
Helixi349 – 351Combined sources3
Turni352 – 356Combined sources5
Beta strandi375 – 377Combined sources3
Beta strandi380 – 386Combined sources7
Helixi387 – 391Combined sources5
Helixi393 – 399Combined sources7
Beta strandi406 – 411Combined sources6
Helixi413 – 416Combined sources4
Turni417 – 420Combined sources4
Helixi421 – 436Combined sources16
Beta strandi440 – 447Combined sources8
Beta strandi450 – 452Combined sources3
Beta strandi458 – 461Combined sources4
Beta strandi464 – 466Combined sources3
Beta strandi468 – 474Combined sources7
Helixi482 – 486Combined sources5
Helixi489 – 505Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5N6HX-ray2.90A/B1-512[»]
5N6LX-ray2.90A/B1-512[»]
5VRGX-ray2.52A2-512[»]
5VRHX-ray2.14A2-512[»]
5XHQX-ray2.59A/B1-508[»]
ProteinModelPortaliP23930
SMRiP23930
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini227 – 476CN hydrolasePROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni425 – 431Could contain a copper-binding motif7

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CE8 Bacteria
COG0815 LUCA
HOGENOMiHOG000264279
InParanoidiP23930
KOiK03820
OMAiPIGEFVP
PhylomeDBiP23930

Family and domain databases

CDDicd07571 ALP_N-acyl_transferase, 1 hit
Gene3Di3.60.110.10, 1 hit
HAMAPiMF_01148 Lnt, 1 hit
InterProiView protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
SUPFAMiSSF56317 SSF56317, 1 hit
TIGRFAMsiTIGR00546 lnt, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit

Sequencei

Sequence statusi: Complete.

P23930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN
60 70 80 90 100
RRPLQSAAIG FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY
110 120 130 140 150
LSLYTGLFAG VLSRLWPKTT WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ
160 170 180 190 200
FGYSQIDGPL KGLAPIMGVE AINFLLMMVS GLLALALVKR NWRPLVVAVV
210 220 230 240 250
LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG QLLNTLKIYY
260 270 280 290 300
NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
310 320 330 340 350
DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI
360 370 380 390 400
LRPLAPFFDL PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILGEQVRDNF
410 420 430 440 450
RPDTDYLLTI SNDAWFGKSI GPWQHFQMAR MRALELARPL LRSTNNGITA
460 470 480 490 500
VIGPQGEIQA MIPQFTREVL TTNVTPTTGL TPYARTGNWP LWVLTALFGF
510
AAVLMSLRQR RK
Length:512
Mass (Da):57,066
Last modified:March 1, 1992 - v1
Checksum:i70CFD6627C286615
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186A → V (PubMed:8905232).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58070 Genomic DNA Translation: CAA41100.1
U82598 Genomic DNA Translation: AAB40859.1
U00096 Genomic DNA Translation: AAC73758.1
AP009048 Genomic DNA Translation: BAA35308.2
PIRiS18194
RefSeqiNP_415190.1, NC_000913.3
WP_000853021.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73758; AAC73758; b0657
BAA35308; BAA35308; BAA35308
GeneIDi946201
KEGGiecj:JW0654
eco:b0657
PATRICifig|1411691.4.peg.1611

Similar proteinsi

Entry informationi

Entry nameiLNT_ECOLI
AccessioniPrimary (citable) accession number: P23930
Secondary accession number(s): P77703
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: March 28, 2018
This is version 145 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health