ID D3UIP7_HELM1 Unreviewed; 436 AA.
AC D3UIP7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 28-JAN-2026, entry version 62.
DE SubName: Full=Putative Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:CBG40372.1};
GN OrderedLocusNames=HMU11170 {ECO:0000313|EMBL:CBG40372.1};
OS Helicobacter mustelae (strain ATCC 43772 / CCUG 25715 / CIP 103759 / LMG
OS 18044 / NCTC 12198 / R85-136P) (Campylobacter mustelae).
OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC Campylobacterales; Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40372.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40372.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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}.
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DR EMBL; FN555004; CBG40372.1; -; Genomic_DNA.
DR RefSeq; WP_013023441.1; NC_013949.1.
DR AlphaFoldDB; D3UIP7; -.
DR STRING; 679897.HMU11170; -.
DR KEGG; hms:HMU11170; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_050649_0_0_7; -.
DR Proteomes; UP000001522; Chromosome.
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; IPR059110; Lnt_campylobact.
DR InterPro; IPR059109; Lnt_membrane_dom.
DR NCBIfam; TIGR00546; lnt; 1.
DR NCBIfam; NF008934; PRK12291.1; 1.
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:CBG40372.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipoprotein {ECO:0000313|EMBL:CBG40372.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001522};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBG40372.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..436
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 436 AA; 49536 MW; C2093363507E3437 CRC64;
MLAPFLRPTR KFLEKSKKSF FFVFLFLLPI WSGAFFFALG DSGGHARGFE TTYIILNSIF
APLAIFAFLR VPSSLGFYFG FYVGIGLFYW VGFSFLYSPA PYLLPIIIIA MGVIYGVVFW
PLLWSEHLFF RIPALFLLSF IHPFGFDWLF GEEFLAYSIF GVGKWSYACV ILGVVLLYKG
GKGFKILAVF LLGFSISQTQ FMGKYEMPLN MELTSTSIGQ SGKWEGQNIQ EIIKYNLSLI
REAVAERKEV IVLPETAFPL ALNLQEDLLE TLKKMSADIG IVVGAMRVQD LQIYNSTYIF
EKGRLQILDK VILAPFGERI PLPKFIAKPL QKLFFGTEEE LSQASKAQDF VLGGKVFRNA
ICYEGTSSLL YEDHPKYVIM ISNNAWFYPS IEPYFQQILL KFYARKYGTI TFHSANFSPS
MVIAPALFAT FSSKSQ
//