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Database: UniProt
Entry: E1QLP7_DESB2
LinkDB: E1QLP7_DESB2
Original site: E1QLP7_DESB2 
ID   E1QLP7_DESB2            Unreviewed;       434 AA.
AC   E1QLP7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
DE            Short=Kdo transferase {ECO:0000256|RuleBase:RU365103};
DE            EC=2.4.99.12 {ECO:0000256|RuleBase:RU365103};
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
GN   OrderedLocusNames=Deba_3129 {ECO:0000313|EMBL:ADK86482.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK86482.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK86482.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC       the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-
CC       Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC       precursor of lipid A. {ECO:0000256|RuleBase:RU365103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC         alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+);
CC         Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603,
CC         ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC         EC=2.4.99.12; Evidence={ECO:0000256|RuleBase:RU365103};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|RuleBase:RU365103}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU365103}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU365103}.
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DR   EMBL; CP002085; ADK86482.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1QLP7; -.
DR   STRING; 644282.Deba_3129; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; dbr:Deba_3129; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_7; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.11720; 3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   PANTHER; PTHR42755:SF1; 3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR42755; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU365103};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103};
KW   Transmembrane {ECO:0000256|RuleBase:RU365103};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365103}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365103"
FT   DOMAIN          37..213
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        63
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            133
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            211
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   434 AA;  45992 MW;  D6D434888D166BFF CRC64;
     MDQSLILYNL ALGLGCAALP PLWLGARLGR RYAEVWPRLG LYRHTPEPGP GPRVWLQAVS
     VGEVAVARAV AERLWELRPD VKLIVSSSTA KGLERAAELF AGRALVAPFP LDMPWAAAAA
     VARLRPQVYA SLETEIWPNL LALLRRSGAG VLLLNGRFSE RSFPGYRRFR WLIAPALARF
     DHLSMIGPAD AQRAVALGAP AARVSVDGNA KYAGLLERAR TSDPAEAAAL LKLDGAPLLV
     AGSMRGGEEA VVMEAFAKVR ARFPRAVLAV APRHLERGRA WLRAAAAAGL TAQSWTHLRP
     DAPRRPETAV VVVDVMGRLM AIYGLGAAAV VGASFVGLGG QNPMEPAAWG KPVAFGPDMS
     DFADASQALI EAGGGRQAAD GAALGDFWLA ALADPALALA WGRAGQGVVE RWSRAAEAAA
     GHIARRLDRR GART
//
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