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Database: UniProt
Entry: F8KR23_HELBC
LinkDB: F8KR23_HELBC
Original site: F8KR23_HELBC 
ID   F8KR23_HELBC            Unreviewed;       429 AA.
AC   F8KR23;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   28-JAN-2026, entry version 61.
DE   SubName: Full=Apolipoprotein N-acyltransferase {ECO:0000313|EMBL:CCB79194.1};
GN   OrderedLocusNames=HBZC1_02080 {ECO:0000313|EMBL:CCB79194.1};
OS   Helicobacter bizzozeronii (strain CIII-1).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB79194.1, ECO:0000313|Proteomes:UP000008387};
RN   [1] {ECO:0000313|EMBL:CCB79194.1, ECO:0000313|Proteomes:UP000008387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIII-1 {ECO:0000313|EMBL:CCB79194.1,
RC   ECO:0000313|Proteomes:UP000008387};
RX   PubMed=21705603; DOI=10.1128/JB.05439-11;
RA   Schott T., Rossi M., Hanninen M.L.;
RT   "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT   from human gastric mucosa.";
RL   J. Bacteriol. 193:4565-4566(2011).
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; FR871757; CCB79194.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8KR23; -.
DR   STRING; 1002804.HBZC1_02080; -.
DR   KEGG; hbi:HBZC1_02080; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_050649_0_0_7; -.
DR   Proteomes; UP000008387; 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   ECO:0000313|EMBL:CCB79194.1};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Lipoprotein {ECO:0000313|EMBL:CCB79194.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCB79194.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..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..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..429
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   429 AA;  49307 MW;  4E96B548140AB90C CRC64;
     MVLCLCDRYW RGYGFVCVCV LLFLLPVYGS LLLAHHPMPL VIFGSFSAPL SVWAYLSVPA
     KRRFFFGFWV GLGLFYWCAL SFRYNDNVFL LPLIMVLIAL CYAVVFYGLL YFNSLLYRIA
     TLWLSSYIHP FGFDWFVPDA FFAYSGFKVD RLSFLGVIVA IALFMQRYKN FMFFKPLYAP
     SKIFAVVLLV LSINWKQSAS ALDPNALKVV QTNTNQKTKW QPEFLDATIA FNLTTIQQAI
     QEKKQVVILP ETAFPIALNK SNLIPTLLSL SQQITIIAGA LYEENDTIYN STYVFDHGDY
     HYAHKVILAP FGERMPLPSF LADYLDRFFF GADVFKLGNA PHFSDMKTQH LDFRPLVCYE
     GTSKPAYENS PPNLVVISNN AWFVPSIEPF LQRMLLKYYA RRFDKTIIHS VNFSPSYILT
     PALLGDRLY
//
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