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Database: UniProt
Entry: A0A0Q9YKF9_9COXI
LinkDB: A0A0Q9YKF9_9COXI
Original site: A0A0Q9YKF9_9COXI 
ID   A0A0Q9YKF9_9COXI        Unreviewed;       256 AA.
AC   A0A0Q9YKF9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE            Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE            EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387};
GN   Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387,
GN   ECO:0000313|EMBL:KRG21167.1};
GN   ORFNames=HT99x_01723 {ECO:0000313|EMBL:KRG21167.1};
OS   Candidatus Berkiella aquae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Candidatus Berkiella.
OX   NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21167.1, ECO:0000313|Proteomes:UP000051497};
RN   [1] {ECO:0000313|EMBL:KRG21167.1, ECO:0000313|Proteomes:UP000051497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HT99 {ECO:0000313|EMBL:KRG21167.1,
RC   ECO:0000313|Proteomes:UP000051497};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC       glycolipid that anchors the lipopolysaccharide to the outer membrane of
CC       the cell. {ECO:0000256|HAMAP-Rule:MF_00387}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC         a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC         [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC         ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00387};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00387}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00387}.
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:KRG21167.1}.
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DR   EMBL; LKAJ01000006; KRG21167.1; -; Genomic_DNA.
DR   RefSeq; WP_075066351.1; NZ_LKAJ02000001.1.
DR   AlphaFoldDB; A0A0Q9YKF9; -.
DR   STRING; 295108.HT99x_01723; -.
DR   PATRIC; fig|1590043.3.peg.1759; -.
DR   OrthoDB; 9807278at2; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000051497; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1.
DR   HAMAP; MF_00387; LpxA; 1.
DR   InterPro; IPR029098; Acetyltransf_C.
DR   InterPro; IPR037157; Acetyltransf_C_sf.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR010137; Lipid_A_LpxA.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR01852; lipid_A_lpxA; 1.
DR   PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00387}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00387};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00387};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00387}; Reference proteome {ECO:0000313|Proteomes:UP000051497};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00387}.
FT   DOMAIN          174..254
FT                   /note="UDP N-acetylglucosamine O-acyltransferase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13720"
SQ   SEQUENCE   256 AA;  27767 MW;  5C54A3D8B012AD9E CRC64;
     MISDKAIIDK SAKIAANVEI SPFSIIGADV EIGEGTWIGP HTVINGPTKI GRNNKIFQFS
     SIGEDPQDKK YAGEPTRLEV GDNNTFRECT TVSRGTTSGG GLTKIGNDNL FMAYVHIAHD
     CHVGNFTTFS NNASLAGHVT VDDHANLGGF VGVHQFCNIG SHCFCAGGSI IVKDVLPFIT
     VSGHPAETYG LNVEGLKRRG FTPDDLTVLK RAYKILYRQG LTLEEAVHKI EAMIPECRHI
     QVIVDFIKKS KRGIAR
//
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