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Database: UniProt
Entry: A0A143DBK3_9PROT
LinkDB: A0A143DBK3_9PROT
Original site: A0A143DBK3_9PROT 
ID   A0A143DBK3_9PROT        Unreviewed;       427 AA.
AC   A0A143DBK3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|ARBA:ARBA00019077, ECO:0000256|RuleBase:RU365103};
DE            Short=Kdo transferase {ECO:0000256|RuleBase:RU365103};
DE            EC=2.4.99.12 {ECO:0000256|ARBA:ARBA00012621, ECO:0000256|RuleBase:RU365103};
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|ARBA:ARBA00031445, ECO:0000256|RuleBase:RU365103};
GN   ORFNames=AY555_01825 {ECO:0000313|EMBL:AMW34117.1};
OS   Haematospirillum jordaniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Haematospirillum.
OX   NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW34117.1, ECO:0000313|Proteomes:UP000076066};
RN   [1] {ECO:0000313|EMBL:AMW34117.1, ECO:0000313|Proteomes:UP000076066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5569 {ECO:0000313|EMBL:AMW34117.1,
RC   ECO:0000313|Proteomes:UP000076066};
RA   Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT   "Complete Genome of H5569, the type strain of the newly described species
RT   Haematospirillium jordaniae.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00003394,
CC       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|ARBA:ARBA00034406,
CC         ECO:0000256|RuleBase:RU365103};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713, 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; CP014525; AMW34117.1; -; Genomic_DNA.
DR   RefSeq; WP_066132663.1; NZ_CP014525.1.
DR   AlphaFoldDB; A0A143DBK3; -.
DR   STRING; 1549855.AY555_01825; -.
DR   GeneID; 53315894; -.
DR   KEGG; hjo:AY555_01825; -.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000076066; 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:UP000076066};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          34..213
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            135
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   427 AA;  47461 MW;  1101C117D79E7554 CRC64;
     MIPFLYHSVV STSAPALRLW LEYRARQGKE DPERLPERRG IASHPRPAGP VLWIHAASVG
     ESLSVLPLLQ SVMTARPSWS AVLTTGTRTS ARLLPSRLHD IGVGRIIHQF VPLDHPRWVG
     RFLDHWQPNL ALWVESELWP NLLKACRERR IASALVNGRM SEHSFQRWRL APALIRDMLS
     GFSLCMGQSP EDTQRLQELG ARNPVCPGNL KYASPPLPVD LDKLEAARNV IKNRPVWLAS
     STHPGEELMA GQVHRAMAAQ IPDLLTIIVP RHPERGEDIA RELMDRGMTV ALRSHGSAPD
     QDCDVWLADT LGELGLFYRL CPVSFIGKSL LGTGGQNPLE PARLGSAVVF GPHMENFAEI
     SIRMLQHRAA IQVPDAEELT RTVQQLLLQP GMRETLTQSA QSFCHQEASV LERIMAHLLP
     LCDSGAS
//
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