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Database: UniProt
Entry: V9TUV2_9PROT
LinkDB: V9TUV2_9PROT
Original site: V9TUV2_9PROT 
ID   V9TUV2_9PROT            Unreviewed;       426 AA.
AC   V9TUV2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   08-MAY-2019, entry version 21.
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   Name=kdtA {ECO:0000313|EMBL:AHC73942.1};
GN   ORFNames=P856_740 {ECO:0000313|EMBL:AHC73942.1};
OS   Candidatus Endolissoclinum faulkneri L5.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Candidatus Endolissoclinum.
OX   NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73942.1};
RN   [1] {ECO:0000313|EMBL:AHC73942.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:AHC73942.1};
RX   PubMed=24324632;
RA   Kwan J.C., Schmidt E.W.;
RT   "Bacterial endosymbiosis in a chordate host: long-term co-evolution
RT   and conservation of secondary metabolism.";
RL   PLoS ONE 8:E80822-E80822(2013).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis.
CC       Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo)
CC       residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-
CC       1,4'-bisphosphate precursor of lipid A.
CC       {ECO:0000256|RuleBase:RU365103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E.
CC         coli) = alpha-Kdo-(2->6)-lipid IVA + 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
CC       biosynthesis. {ECO:0000256|RuleBase:RU365103}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU365103}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU365103}.
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DR   EMBL; CP006745; AHC73942.1; -; Genomic_DNA.
DR   RefSeq; WP_025300819.1; NZ_CP006745.1.
DR   STRING; 1401328.P856_740; -.
DR   EnsemblBacteria; AHC73942; AHC73942; P856_740.
DR   KEGG; efk:P856_740; -.
DR   PATRIC; fig|1401328.3.peg.746; -.
DR   KO; K02527; -.
DR   OrthoDB; 1163086at2; -.
DR   UniPathway; UPA00958; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.11720; -; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   PANTHER; PTHR42755; PTHR42755; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365103};
KW   Cell membrane {ECO:0000256|RuleBase:RU365103};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Transferase {ECO:0000256|RuleBase:RU365103,
KW   ECO:0000313|EMBL:AHC73942.1}.
FT   DOMAIN       34    207       Glycos_transf_N. {ECO:0000259|Pfam:
FT                                PF04413}.
FT   DOMAIN      245    397       Glycos_transf_1. {ECO:0000259|Pfam:
FT                                PF00534}.
SQ   SEQUENCE   426 AA;  47195 MW;  B0ABD4EBACD54AE7 CRC64;
     MILQIYKALV TFSGLFLDVY FRLRLVRGKE NKFRLNERRG IATKSRPSGR LVWLHAVSVG
     EAAGLLALIK IIHDTKPWII LLLTTCTVTS GDLIRKLLPK GVIHQFIPID RPAWVGRFLD
     YWNPDLAIWM ESDLWPTMVT EANARGIYMI IVSGRLSFRA FQRWKSIGSL AKPLFSAFDL
     VLAASHEQVR RFFALGCVDV RYVGNLKDSI VPPKVDIKIA AALRNSITYR PVWLAASTHR
     GEESLVLDAH AQIAKTKPNL LTVIVPRHTN RSDEIARIVQ RRGLTLVRRS ANQSIKERTS
     VYLADTMGEI AIFYSVIPVT FLAGSMVKVG GHNPIEASYC GTAIVFGPLM ENNRESADAL
     IAAGAAREVN DAASLAKTVE DLLDDPITAN EMGACARRVA IARAIKINSI LEVIDPILPE
     KPLGVT
//
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