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Database: UniProt
Entry: C5ZXZ2_9HELI
LinkDB: C5ZXZ2_9HELI
Original site: C5ZXZ2_9HELI 
ID   C5ZXZ2_9HELI            Unreviewed;       421 AA.
AC   C5ZXZ2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   28-JAN-2026, entry version 61.
DE   SubName: Full=Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:EES90010.1};
GN   Name=cutE {ECO:0000313|EMBL:EES90010.1};
GN   ORFNames=HCAN_1301 {ECO:0000313|EMBL:EES90010.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES90010.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES90010.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 98-5491 {ECO:0000313|EMBL:EES90010.1,
RC   ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(2009).
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; CM000776; EES90010.1; -; Genomic_DNA.
DR   RefSeq; WP_006656352.1; NZ_DS990370.1.
DR   AlphaFoldDB; C5ZXZ2; -.
DR   STRING; 537970.HCAN_1301; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_050649_0_0_7; -.
DR   OrthoDB; 9804277at2; -.
DR   Proteomes; UP000007032; 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   Pfam; PF00795; CN_hydrolase; 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   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..421
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   421 AA;  48606 MW;  9C72A76B44B95473 CRC64;
     MIGIFSSNKT KLTQITLGIL AALFLSAFIY EEHFFYTWKH PFFSSFFAIL GFFMLLHFSR
     LSAFICGSSI GILWFYWIGL SFRFYNLTYL IPLVWIFVAL IFGIFFLALC YFKNPIYRIS
     ALLCASFIHP FGFNWFIPEL TLTQSYFFSS KSILALLLIS LIIFGFLIQK RFYKIGFFGL
     ILGLFGIGLF SQTLYPTSKE SPLKIKTIST NIPQNLRWDS NNLKQIIDEN FRLIQQAKQE
     NYDLIILPET AFPIALNAED SLLRILQDLS QDLAILTGAI HKQGNSYYNS AYLFYEGKMQ
     IFDKIILVPF GEKIPLPQFL VNLINQIFFK GGVDFTTNSN QKPNSTILQN QHFQIAICYE
     ATRQEFYQDS PSFLIAISNN AWFKPSIEPT LQKLLMQYFS LNYGTTIYHS SNGSQDFILS
     P
//
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