ID T1D0V7_9HELI Unreviewed; 543 AA.
AC T1D0V7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE SubName: Full=Apolipoprotein N-acyltransferase/ Copper homeostasis protein CutE {ECO:0000313|EMBL:GAD18841.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:GAD18841.1};
GN ORFNames=HFN_2253 {ECO:0000313|EMBL:GAD18841.1};
OS Helicobacter fennelliae MRY12-0050.
OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC Campylobacterales; Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD18841.1, ECO:0000313|Proteomes:UP000018143};
RN [1] {ECO:0000313|EMBL:GAD18841.1, ECO:0000313|Proteomes:UP000018143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD18841.1,
RC ECO:0000313|Proteomes:UP000018143};
RA Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA Kuroda M., Shibayama K.;
RT "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT Isolated from a Bacteremia Patient.";
RL Genome Announc. 1:e00512-13(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00010065}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD18841.1}.
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DR EMBL; BASD01000009; GAD18841.1; -; Genomic_DNA.
DR RefSeq; WP_023947765.1; NZ_BASD01000009.1.
DR AlphaFoldDB; T1D0V7; -.
DR STRING; 1325130.HFN_2253; -.
DR eggNOG; COG0815; Bacteria.
DR OrthoDB; 9804277at2; -.
DR Proteomes; UP000018143; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR059109; Lnt_membrane_dom.
DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR Pfam; PF26365; ApoNAT_membrane; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:GAD18841.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipoprotein {ECO:0000313|EMBL:GAD18841.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAD18841.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..543
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 411..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 61800 MW; B535E72FD2566A02 CRC64;
MNIFVFSETF KAPTFKKLLK FRKKEWIAFS VVIACSAIFA FLFCLGVYVF ALCSDLFAFV
PESMPDVIIP QSQTLSAQNY IGATLMSICA MLSIAVWFIV PKALRFWFGF FCGVFLFYWI
GLSFRYSPLP FVGLFVPLCI GLVYGVLIFF ALYYESKLYR LITLVLMSFI HPFGFDWFMP
PALLSYSFFG VSWWHFVCLE CAIALFLVRS SKFFMLLGLV LFVCSIDSTT FQIHKTDDFL
TQKTQIIQTN LPQDLKWNQQ SLNLIVTNVL SQIDKAIRES SAMIIFPETM LPFVLNADSA
YSRTILEILK DKSSHIAIVI GSFSQQEDRI YNSTYVLYRH QVQILNKVVL APFGEKIPLP
DFLAKPLYRI FFGMEDSLFF ASEPQDFELF GYTFRNAICY EGTTSKIYAP RTTPAQDASK
NIDSAKATTS AESTIQQNNS AQSTPVRNVD STQPTHSSHS PQFVVMISNN GWFAPSIESH
LQRMLLKYYA RLNHSFILHS TNRSESGIIT PYLFGDMPTT YTLSPFSPSQ AHASQNTNSH
KGF
//
